33rd ICHO Preparatory

33rd International Chemistry Olympiad ∗ Preparatory Problems
Preparatory Problems
33rd International Chemistry Olympiad
Edited by Savita Ladage and Arvind Kumar
Copyright  2001 Homi Bhabha Centre for Science Education
Printed in Mumbai, India.
This publication is not for sale and may not be reproduced for lending, hire or sale. Teachers
may, however, reproduce material taken from the publication for use with their students for
the purpose of solving problems in chemistry.
Homi Bhabha Centre for Science Education

Tata Institute of Fundamental Research
V.N.Purav Marg, Mankhurd
Mumbai - 400088
India.
Mumbai, India, July 2001
ii
Contents
From the 33rd IChO Secretariat iv
Preface v
Draft Syllabus for the International Chemistry Olympiad vii-xvi
Theoretical Problems 1-36
Problem 1 Water
Problem 2 van der Waals gases
Problem 3 Rates and reaction mechanisms
Problem 4 Enzyme catalysis
Problem 5 Schrödinger equation
Problem 6 Atomic and molecular orbitals
Problem 7 Fission
Problem 8 Radioactive decay
Problem 9 Redox reactions
Problem 10 Solubility of sparingly soluble salts
Problem 11 Spectrophotometry
Problem 12 Reactions in buffer medium
Problem 13 Identification of an inorganic compound
Problem 14 Ionic and metallic structures
Problem 15 Compounds of nitrogen
Problem 16 Structure elucidation with stereochemistry
Problem 17 Organic spectroscopy and structure determination
Problem 18 Polymer synthesis
Problem 19 Organic synthesis involving regioselection
Problem 20 Carbon acids
Problem 21 Amino acids and enzymes
Problem 22 Coenzyme chemistry
Problem 23 Protein folding
Problem 24 Protein sequencing
Practical Problems 37-48
Safety Regulations
Problem 25 Determination of aspirin in the given sample

Problem 26 Synthesis of 1-phenyl-azo-2-naphthol C16H12ON2
Problem 27 Estimation of calcium in a sample solution
Problem 28 Estimation of methyl ketone by back titration
Problem 29 Estimation of phenol in the given sample
Problem 30 Determination of amount of Fe (III) present in the given sample
Worked Solutions to Problems 49-111
Mumbai, India, July 2001 iii

33rd IChO National Scientific Committee
Prof. N. Sathyamurthy Indian Institute of Technology, Kanpur

Chairperson
Prof. K. D. Deodhar Indian Institute of Technology, Mumbai

Prof. S. Durani Indian Institute of Technology, Mumbai
Prof. S. R. Gadre University of Pune, Pune
Prof. R. V. Hosur Tata Institute of Fundamental Research, Mumbai
Prof. Arvind Kumar Homi Bhabha Centre for Science Education (TIFR), Mumbai
Dr. Savita Ladage Homi Bhabha Centre for Science Education (TIFR), Mumbai
Prof. Uday Maitra Indian Institute of Science, Bangalore
Prof. R. N. Mukherjee Indian Institute of Technology, Kanpur
Dr. R. P. Patel Bhabha Atomic Research Centre, Mumbai
Dr. S. K. Patil Bhabha Atomic Research Centre, Mumbai (formerly)
Prof. N. S. Punekar Indian Institute of Technology, Mumbai
Prof. M. N. S. Rao Indian Institute of Technology, Chennai
Dr. K. B. Sainis Bhabha Atomic Research Centre, Mumbai
Prof. S. D. Samant University Dept of Chemical Technology, Mumbai
Prof. B. L. Tembe Indian Institute of Technology, Mumbai
Prof. Y. D. Vankar Indian Institute of Technology, Kanpur
Supporting Scientific Staff
Ms. Swapna Narvekar Homi Bhabha Centre for Science Education (TIFR), Mumbai
Mr. Rajesh Kumar Homi Bhabha Centre for Science Education (TIFR), Mumbai
iv
SYLLABUS OF THE INTERNATIONAL CHEMISTRY OLYMPIAD
Level 1: These topics are included in the overwhelming majority of secondary

school chemistry programs and need not be mentioned in the
preparatory problems
Level 2: These topics are included in a substantial number of secondary school

programs and maybe used without exemplification in the preparatory
problems.
Level 3: These topics are not included in the majority of secondary school
programs and can only be used in the competition if examples are
given in the preparatory problems
1 INORGANIC CHEMISTRY 1.4 Structures
1.1 Electronic configuration of atoms 1.4.1 simple molecular structures 2

and ions 1.4.2 simple molecular structures with
central atom exceeding octet rule 3
1.1.1 main groups 1 1.4.3 ionic crystal structures 3
1.1.2 transition metals 2 1.4.4 metal structures 3
1.1.3 lanthanide and actinide metals 3 1.4.5 stereochemistry 3
1.1.4 Pauli exclusion principle 1
1.1.5 Hund's rule 1 1.5 Nomenclature
1.2 Trends in the periodic table 1.5.1 oxidation number 1

(main groups) 1.5.2 main group compounds 1
1.5.3 transition metal compounds 1
1.2.1 electronegativity 1 1.5.4 simple metal complexes 2
1.2.2 electron affinity 2 1.5.5 multicenter metal complexes 3
1.2.3 first ionisation energy 2
1.2.4 atomic size 1 1.6 Chemical calculations
1.2.5 ionic size 2
1.2.6 highest oxidation number 1 1.6.1 balancing equations 1
1.6.2 stoichiometric calculations 1
1.3 Trends in physical properties 1.6.3 mass and volume relations 1
(main groups) 1.6.4 empirical formula 1
1.6.5 Avogadro's number 1
1.3.1 melting point 1 1.6.6 concentration calculations 1
1.3.2 boiling point 1
1.3.3 metal character 1 1.7 Isotopes
1.3.4 magnetic properties 2
1.3.5 thermal properties 3 1.7.1 counting of nucleons 1
1.3.6 law of Dulong and Petit 1 1.7.2 radioactive decay 1
1.3.7 electrical conductivity 3 1.7.3 nuclear reactions (alpha, beta,
gamma, neutrino) 2
Mumbai, India, July 2001 v

1.8 Natural cycles oxides with water and

stoichiometry of resulting acids 1
1.8.1 nitrogen 2 1.10.18 reactions of halogens with water 2
1.8.2 oxygen 2 1.10.19 reactivity and oxidising power of
1.8.3 carbon 2 halogens decrease from F2 to I2 1
1.10.20 differences of chemistry between
1.9 s-Block row 4 and row 3 elements 3
1.9.1 Products of reactions of group I 1.11 d-Block

and II metals
1.11.1 common oxidation states of the
1.9.1.1 with water, basicity of the common d-block metals are Cr(III),
products 1 Cr(VI), Mn(II), Mn(IV), Mn(VII),
1.9.1.2 with halogens 1 Fe(II), Fe(III), Co(II), Ni(II), Cu(I),
1.9.1.3 with oxygen 2 Cu(II), Ag(I), Zn(II), Hg(I), and
1.9.2 heavier s-block elements are Hg(II) 1
more reactive 1 1.11.2 colours of the listed common
1.9.3 lithium combines with H2 and N2 ions in aqueous solutions 2
forming LiH and Li3N 2 1.11.3 other oxidation states and chemistry
of other d-block elements 3
1.10 p-Block 1.11.4 Cr, Mn, Fe, Co, Ni, Zn dissolve in
dilute HCl; Cu, Ag, Hg do not
1.10.1 stoichiometry of simplest dissolve 1
non-metal hydrides 1 1.11.5 products of dissolution are (2+)
1.10.2 properties of metal hydrides 3 cations 2
1.10.3 acid-base properties of CH4, NH3, 1.11.6 passivaion of Cr, Fe (and also Al) 2
H2O, H2S, and hydrogen l.11.7 Cr(OH)3 and Zn(OH)2 are amphoteric,
halides HX 1 other common hydroxides are not 1
1.10.4 NO reacts with O2 to form NO2 1 1.11.8 MnO4-, CrO42-, Cr2O72- are
1.10.5 equilibrium between NO2 and strong oxidants 1
N2O4 1 1.11.9 products of reduction of MnO4-
1.10.6 products of reaction of NO2 with depending on pH 2
water 1 1.11.10 polyanions other than Cr2O72- 3
1.10.7 HNO2 and its salts are reductants 1
1.10.8 HNO3 and its salts are oxidants 1 1.12 Other inorganic problems
1.10.9 N2H4 is a liquid and reductant 3
1.10.10 there exist acids like H2N2O2, 1.12.1 industrial production of H2SO4,
HN3 3 NH3, Na2CO3, Na, Cl2, NaOH, 1
1.10.11 reactions of HNO3 with different 1.12.2 chemistry of lanthanides and
metals and reductants 3 actinides 3
1.10.12 reaction of Na2S2O3 with iodine 2 1.12.3 chemistry of noble gases 3
1.10.13 other thioacids, polyacids,
peroxoacids 3 2. PHYSICAL CHEMISTRY
1.10.14 B(III), Al(III), Si(IV), P(V),
S(IV), S(VI), O(-II), F(-I), Cl(-I), 2.1 Chemical equilibria
Cl(I), Cl(III), Cl(V), Cl(VII)
are normal oxidation states of 2.1.1 dynamical model of chemical
2nd and 3rd row elements equilibrium 1
in compounds with 2.1.2 chemical equilibria expressed in terms
halogens and in oxoanions 1 of relative concentrations 1
1.10.15 compounds of non-metals with 2.1.3 chemical equilibria expressed in
other oxidation states 3 terms of partial pressures 2
1.10.16 the preferred oxidation states 2.1.4 the relationship between equilibrium
are Sn(II), Pb(II) and Bi(III) 2 constants for ideal gases expressed
1.10.17 products of reactions of non-metal in different ways (concentration,
vi
pressure, mole fraction) 3 2.4.10 Arrhenius equation, activation

2.1.5 relation of equilibrium constant energy (definition) 2
and standard Gibbs energy 3 2.4.11 calculation of rate constant
for 1st order reaction 2
2.2 Ionic equilibria 2.4.12 calculation of rate constant for
second, third order reaction 3
2.2.1 Arrhenius theory of acids and 2.4.13 calculation of activation energy
bases 1 from experimental data 3
2.2.2 Broensted-Lowry theory, conjugated 2.4.14 basic concepts of collision theory 3
acids and bases 1 2.4.15 basic concepts of transition state
2.2.3 definition of pH 1 theory 3
2.2.4 ionic product of water 1 2.4.16 opposing, parallel and consecutive
2.2.5 relation between Ka and Kb for reactions 3
conjugated acids and bases 1
2.2.6 hydrolysis of salts 1 2.5 Thermodynamics (First law)
2.2.7 solubility product - definition 1
2.2.8 calculation of solubility (in water) 2.5.1 system and its surroundings 2
from solubility product 1 2.5.2 energy, heat and work 2
2.2.9 calculation of pH for weak acid from 2.5.3 relation between enthalpy and
Ka 1 energy 2
2.2.10 calculation of pH for 10-7 mol dm-3 2.5.4 heat capacity – definition 2
HCl solution 2 2.5.5 difference between Cp and Cv
2.2.11 calculation of pH for multiprotic (ideal gas only) 2
acids 2 2.5.6 Hess law 2
2.2.12 calculation of pH for weak acid 2.5.7 Born-Haber cycle for ionic
mixtures 3 compounds 3
2.2.13 definition of activity coefficient 2 2.5.8 lattice energies – approximate
2.2.14 definition of ionic strength 3 calculations (e.g. Kapustinski
2.2.15 Debye-Hückel formula 3 equation) 3
2.5.9 use of standard formation
enthalpies 2
2.3 Electrode equilibria 2.5.10 heats of solution and solvation 2
2.5.11 bond energies - definition and uses 2
2.3.1 electromotive force (definition) 1
2.3.2 first kind electrodes 1 2.6 Thermodynamics (Second law)
2.3.3 standard electrode potential 1
2.3.4 Nernst equation 2 2.6.1 entropy, definition (q/T) 2
2.3.5 second kind electrodes 2 2.6.2 entropy and disorder 2
2.3.6 relation between ∆G and 2.6.3 relation S = k ln W 3
electromotive force 3 2.6.4 relation ∆G = ∆H - T∆S 2
2.6.5 ∆G and directionality of changes 2
2.4 Kinetics of homogeneous reactions
2.7 Phase systems
2.4.1 factors influencing reaction rate 1
2.4.2 rate equation 1 2.7.1 ideal gas law 1
2.4.3 rate constant 1 2.7.2 van der Waals gas law 3
2.4.4 order of reactions 2 2.7.3 definition of partial pressure 1
2.4.5 1st order reactions: time dependence 2.7.4 temperature dependence of the
of concentration 2 vapour pressure of liquid 2
2.4.6 1st order reactions: half-life 2 2.7.5 Clausius-Clapeyron equation 3
2.4.7 1st order reactions: relation between 2.7.5 reading phase diagrams:
half-life and rate constant 2 triple point 3
2.4.8 rate-determining step 2 2.7.6 phase diagrams:
2.4.9 molecularity 2 critical temperature 3
Mumbai, India, July 2001 vii

2.7.8 liquid-vapour system (diagram) 3 3.5 Arenes and heterocycles

2.7.9 liquid-vapour: ideal and non-ideal
systems 3 3.5.1 formula of benzene 1
2.7.10 liquid-vapour: use in fractional 3.5.2 delocalization of electrons 1
distillation 3 3.5.3 stabilization by resonance 1
2.7.11 Henry's law 2 3.5.4 Hückel (4n + 2) rule 3
2.7.12 Raoult's law 2 3.5.5 aromaticity of heterocycles 3
2.7.13 deviations from Raoult's law 3 3.5.6 nomenclature of heterocycles
2.7.14 boiling point elevation law 2 (IUPAC) 3
2.7.15 freezing point depression, 3.5.7 polycyclic aromatic compounds 3
determination of molar mass 2 3.5.7 effect of first substituent on
2.7.16 osmotic pressure 2 reactivity 2
2.7.17 partition coefficient 3 3.5.9 effect of first substituent on
2.7.18 solvent extraction 3 direction of substitution 2
2.7.19 basic principles of chromatography2 3.5.10 explanation of substituent effects 3
3. ORGANIC CHEMISTRY 3.6 Halogen compounds
3.1 Alkanes 3.6.1 hydrolytic reactions 2

3.6.2 exchange of halogens 3
3.1.1 isomers of butane 1 3.6.3 reactivity (primary vs secondary vs
3.1.2 naming (IUPAC) 1 tertiary) 2
3.1.3 trends in physical properties 1 3.6.4 ionic mechanism of substitution 2
3.1.4 substitution (e.g. with Cl2) 3.6.5 side products (elimination) 2
3.1.4.1 products 1 3.6.6 reactivity (aliphatic vs aromatic) 2
3.1.4.2 free radicals 2 3.6.7 Wurtz (RX + Na) reaction 3
3.1.4.3 initiation/termination of the 3.6.8 halogen derivatives and pollution 3
chain reaction 2
3.7 Alcohols and phenols
3.2 Cycloalkanes
3.7.1 hydrogen bonding - alcohols vs
3.2.1 names 1 ethers 1
3.2.2 strain in small rings 2 3.7.2 acidity of alcohols vs phenols 2
3.2.3 chair/boat conformation 2 3.7.3 dehydration to alkenes 1
3.7.4 dehydration to ethers 2
3.3 Alkenes 3.7.5 esters with inorganic acids 2
3.7.6 iodoform reaction 2
3.3.1 planarity 1 3.7.7 reactions of primary/secondary/
3.3.2 E/Z (cis-trans) isomerism 1 tertiary: Lucas reagent 2
3.3.3 Addition of Br2 and HBr 3.7.8 formula of glycerin 1
3.3.3.1 products 1
3.3.3.2 Markovnikoff's rule 2 3.8 Carbonyl compounds
3.3.3.3 carbonium ions in addition
reaction 3 3.8.1 nomenclature 1
3.3.3.4 relative stability of carbonium ions 3 3.8.2 keto/enol tautomerism 2
3.3.3.5 1,4-addition to alkadiene 3
3.8.3 Preparation of carbonyl compounds
3.8.3.1 oxidation of alcohols 1
3.4 Alkynes 3.8.3.2 from carbon monoxide 3
3.4.1 linear geometry 1 3.8.4 Reaction of carbonyl compounds

3.4.2 acidity 2 3.8.4.1 oxidation of aldehydes 1
3.4.3 differences in chemical properties 3.8.4.2 reduction with Zn metal 2
between alkenes and alkynes 3 3.8.4.3 addition of HCN 2
3.8.4.4 addition of NaHSO3 2
viii
3.8.4.5 addition of NH2OH 2 3.11.6 mechanism of Hoffmann

3.8.4.6 aldol condensation 3 rearrangement in acidic/basic
3.8.4.7 preparation of acetates 2 medium 3
3.8.4.8 Cannizzaro (PhCH2OH 3.11.7 basicity amines vs amides 2
disproportionation) 3 3.11.7 diazotation products of
3.8.4.9 Grignard reaction 2 aliphatic amines 3
3.8.4.10 Fehling (Cu2O) and Tollens 3.11.9 diazotation products of
(Ag mirror) 2 aromatic amines 3
3.11.10 dyes:colour vs structure
3.10 Carboxylic acids (chromophore groups) 3
3.11.11 nitrocompounds: aci/nitro
3.10.1 inductive effect and strength 2 tautomerism 3
3.10.2 equivalence of oxygen atoms in 3.11.12 Beckmann(oxime-amide)
anions 2 rearrangements 3
3.10.3 Preparation and reactions of
carboxylic acids 3.12 Some large molecules
3.10.3.1 preparation from esters 2
3.10.3.2 preparation from nitriles 2 3.12.1 hydrophilic/hydrophobic groups 2
3.10.3.3 products of reaction with 3.12.2 micelle structure 3
alcohols (esters) 1 3.12.3 preparation of soaps 1
3.10.3.4 mechanism of esterification 2 products of polymerization of:
3.10.3.5 isotopes in mechanism 3.12.4 styrene 2
elucidation 3 3.12.5 ethene 1
3.10.3.6 nomenclature of acid halides 2 3.12.6 polyamides 3
3.10.3.7 preparation of acid chlorides 2 3.12.7 phenol + aldehydes 3
3.10.3.8 preparation of amides from 3.12.8 polyuretanes 3
acid chlorides 2 3.12.9 polymers cross linking 3
3.10.3.9 preparation of nitriles from 3.12.10 chain mechanism of polymer
acid chlorides 3 formation 2
3.10.3.10 properties and preparation of 3.12.11 rubber composition 3
anhydrides 2
3.10.3.11 oxalic acid, name and formula 1
3.10.3.12 multifunctional acids 4. BIOCHEMISTRY
(e.g. hydroxyacids, ketoacids) 2
3.10.3.13 polycarboxylic acids 2 4.1 Amino acids and peptides
3.10.3.14 optical activity (e.g. lactic acid 2
3.10.3.15 R/S nomenclature 3 4.1.1 ionic structure of aminoacids 1
3.10.3.16 plant and animal fats, 4.1.2 isoelectric point 2
differences 2 4.1.3 20 aminoacids (classification in
groups) 2
3.11 Nitrogen compounds 4.1.4 20 aminoacids (names and
structures) 3
3.11.1 basicity of amines 1 4.1.5 ninhydrin reaction (including
3.11.2 comparing aliphatic vs aromatic 2 equation) 3
3.11.3 names: primary, secondary, 4.1.6 separation by chromatography 3
tertiary, quaternary amines 2 4.1.7 separation by electrophoresis 3
3.11.4 identificationof primary/sec./tert./ 4.1.8 peptide linkage 1
quaternary amines in laboratory 3
3.11.5 Preparation of amines 4.2 Proteins
3.11.5.1 from halogen compounds 2
3.11.5.2 from nitro compounds (e.g. PhNH2 4.2.1 primary structure of proteins 1
from PhNO2) 3 4.2.2 -S-S- bridges 3
3.11.5.3 from amides (Hoffmann) 3 4.2.3 sequence analysis 3
4.2.4 secondary structures 3
Mumbai, India, July 2001 ix

4.2.5 details of alpha-helix structure 3 4.5.13 detailed Calvin cycle 3

4.2.6 tertiary structure 3
4.2.7 denaturation reaction by change 4.6 Krebs cycle and respiration chain
of pH, temperature, metals,
ethanol 2 4.6.1 formation of CO2 in the cycle
4.2.8 quaternary structure 3 (no details) 3
4.2.9 separation of proteins (molecule 4.6.2 intermediate compounds in the
size and solubility) 3 cycle 3
4.2.10 metabolism of proteins (general) 3 4.6.3 formation of water and ATP
4.2.11 proteolysis 3 (no details) 3
4.2.12 transamination 3 4.6.4 FMN and cytochromes 3
4.2.13 four pathways of catabolism of 4.6.5 calculation of ATP amount for
amino acids 3 1 mole of glucose 3
4.2.14 decarboxylation of amino acids 3
4.2.15 urea cycle (only results) 3 4.7 Nucleic acids and protein synthesis
4.3 Fatty acids and fats 4.7.1 pyrimidine, purine 2

4.7.2 nucleosides and nucleotides 3
4.3.1 IUPAC names from C4 to C18 2 4.7.3 formulas of all pyrimidine and
4.3.2 trivial names of most important purine bases 3
(ca. 5) fatty acids 2 4.7.4 difference between ribose and
4.3.3 general metabolism of fats 2 2-deoxyribose 3
4.3.4 beta-oxidation of fatty acids 4.7.5 base combination CG and AT 3
(formulas and ATP balance) 3 4.7.6 base combination CG and AT –
4.3.5 fatty acids and fats anabolism 3 (hydrogen bonding structure) 3
4.3.6 phosphoglycerides 3 4.7.7 difference between DNA and RNA 3
4.3.7 membranes 3 4.7.8 difference between mRNA and
4.3.8 active transport 3 tRNA 3
4.7.9 hydrolysis of nucleic acids 3
4.4 Enzymes 4.7.9 semiconservative replication of
DNA 3
4.4.1 general properties, active centres 2 4.7.11 DNA-ligase 3
4.4.2 nomenclature, kinetics, coenzymes, 4.7.12 RNA synthesis (transcription)
function of ATP, etc. 3 without details 3
4.7.13 reverse transcriptase 3
4.5 Saccharides 4.7.14 use of genetic code 3
4.7.15 start and stop codons 3
glucose and fructose: 4.7.16 translation steps 3
4.5.1 - chain formulas 2
4.5.2 - Fischer projections 2 4.8 Other biochemical problems
4.5.3 - Haworth formulas 3
4.5.4 osazones 3 4.8.1 hormones, regulation 3
4.5.5 maltose as reducing sugar 2 4.8.2 hormones, feedback 3
4.5.6 difference between starch and 4.8.3 insulin, glucagon, adrenaline 3
cellulose 2 4.8.4 mineral metabolism (no details) 3
4.5.7 difference between alpha- and 4.8.5 ions in blood 3
beta-D glucose 2 4.8.6 buffers in blood 3
4.5.8 metabolism from starch to acetyl 4.8.7 haemoglobin; function and skeleton 3
-CoA 3 4.8.8 haemoglobin; diagram of oxygen
4.5.9 pathway to lactic acid or to absorption 3
ethanol; catabolism of glucose 3 4.8.9 steps in clotting the blood 3
4.5.10 ATP balance for the above 4.8.10 antigens and antibodies 3
pathways 3 4.8.11 blood groups 3
4.5.11 photosynthesis (products only) 2 4.8.12 acetyl choline, structure and
4.5.12 light and dark reaction 3 functions 3
x
OTHER PROBLEMS 8. Instrumental methods of determining

structure
5. Analytical chemistry
8.1 UV-VIS spectroscopy
5.1 choice of indicators for acidimetry 1
5.2 titration curve; pH (strong and weak 8.1.1 identification of aromatic compound 3
acid) 2 8.1.2 identification of chromophore 3
5.3 EMF (redox titration) 2
5.4 calculation of pH of simple 8.2 Mass spectra
buffer solution 2
5.5 identification of Ag+, Ba2+, Cl-, SO42- 1 recognition of:
5.6 identification of Al3+, NO2-, NO3-, Bi3+2
5.7 identification of VO3-, ClO3-, Ti4+ 3 8.2.1- molecular ion 3
5.8 use of flame tests for identification 8.2.2- fragments with a help of a table 3
of K, Ca a Sr 1 8.2.3 typical isotope distribution 3
5.9 Beer-Lambert law 2
8.3 Infrared spectra
6. Complexes
8.3.1 interpretation using a table of
6.1 writing down complexation reactions1 group frequencies 3
6.2 definition of coordination number 1 8.3.2 recognition of hydrogen bonds 3
6.3 prediction of coordination number of 8.3.3 Raman spectroscopy 3
complex ions and molecules 3
6.4 complex formation constants 8.4 NMR
(definition) 2
6.5 Eg and T2g terms: high and low spin 8.4.1 interpretation of simple
octahedral complexes 3 spectrum (like ethanol) 3
6.6 calculation of solubility of AgCl in NH3 8.4.2 spin-spin coupling 3
(from Ks and constants β) 3 8.4.3 coupling constants 3
6.7 cis and trans forms 3 8.4.4 identification of o- and p-
substituted benzene 3
7. Theoretical chemistry 8.4.5 13C- NMR 3
7.1 energy levels of hydrogen atom 8.5 X-rays

(formula) 2
7.2 square of the wave function 8.5.1 Bragg law 3
and probability 3 8.5.2 electron density diagram 3
7.3 understanding the simplest 8.5.3 coordination number 3
Schrödinger equation 3 8.5.4 unit cell 3
7.4 n, l, m quantum numbers 2
7.5 shape of p-orbitals 2
7.6 d orbital stereoconfiguration 3 structures:
7.7 molecular orbital diagram: 8.5.5- of NaCl 3
H2 molecule 2 8.5.6- of CsCl 3
7.8 molecular orbital diagram: 8.5.7- close-packed (2 types) 3
N2 and O2 molecules 3 8.5.8 determining of the Avogadro
7.9 bond orders in O2, O2+, O2- 3 constant from X-ray data 3
7.9 unpaired electrons and
paramagnetism 2 8.6 Polarimetry
7.10 Hückel theory for aromatic
compounds 3 8.6.1 calculation of specific rotation angle 3
7.12 Lewis acids and bases 2
7.13 hard and soft Lewis acids 3
Mumbai, India, July 2001 xi

Syllabus for the Experimental Part of the IChO Competition
Level 1 is assigned to the basic experimental activities which are supposed to

be mastered by competitors very well.
Level 2 is assigned to the activities which are parts of school experimental
exercises in developed countries and the authors of IChO tasks may
incorporate them into the tasks without being bounded to mention it in
advance.
Level 3 is assigned to such activities which are not in the chemistry syllabus in
the majority of participating countries and the authors are obliged to
mention them in the set of preparatory tasks.
1. Synthesis of inorganic and 1.24 washing of precipitates by

organic compounds decantation 1
1.25 washing of precipitates on a filter 2
1.1 heating with burners and hotplates 1 1.26 drying of precipitates on a filter
1.2 heating of liquids 1 with appropriate solvents 2
1.3 handling the work with inflammable 1.27 recrystallization of substances from
substances and materials 1 aqueous solution 1
1.4 measuring of masses 1.28 recrystallization of substances from
(analytical balance) 1 a known organic solvent 2
1.5 measuring of volumes of liquids 1.29 practical choice of an appropriate
(measuring cylinder, pipette, burette)1 solvent for recrystallization of
1.6 preparation of solutions a substance 3
from a solid compound and solvent 1 1.30 drying of substances in a drying
1.7 mixing and dilution of solutions 1 box 2
1.8 mixing and stirring of liquids 1 1.31 drying of substances in a
1.9 using mixer and magnetic stirrer 2 desiccator 2
1.10 using a dropping funnel 1 1.32 connecting and using of a gas
1.11 syntheses in flat bottom vessels – washing bottle 2
general principles 1 1.33 extraction with an inmiscible
1.12 syntheses in round bottom vessels – solvent 1
general principles 1
1.13 syntheses in a closed apparatus –
general principles 1 2. Identification of inorganic and
1.14 using microscale equipment for organic compounds- general
synthesis 3 principles
1.15 apparatus for heating of
reaction mixture under reflux 2 2.1 test-tube reactions 1
1.16 apparatus for distillation of liquids at 2.2 technique of reactions performed in a
normal pressure 2 dot dish and on a filter paper 1
1.17 apparatus for distillation of liquids at 2.3 group reactions of some cations and
reduced pressure 3 anions specified by the organizer 2
1.18 apparatus for steam distillation 3 2.4 selective reactions of some cations
1.19 filtration through flat paper filter 1 and anions specified by the
1.20 filtration through a folded paper filter1 organizer 2
1.21 handling a water vacuum pump 1 2.5 specific reactions of some cations and
1.22 filtration through a Büchner funnel 1 anions specified by the organizer 3
1.23 suction through a glass filter 1 2.6 identification of elements by flame
coloration (using a platinum wire/MgO
xii
rod, Co-glass) 2 3.11 other types of determinations on basis

2.7 using a hand spectroscope/ of redox reactions 3
Bunsen spectroscope 3 3.13 complexometric determinations 3
2.8 melting point determination with Kofler 3.14 color transitions of solutions
or similar type of apparatus 3 at complexometric determinations 3
2.9 qualitative evidence of basic functional 3.15 volumetric determinations
groups of organic substances specified on basis of precipitation reactions 3
by the organizer 2 3.16 thermometric titration 3
2.10 exploitation of some specific reactions
for identification of organic compounds 4. Special measurements and
(specified by the organizer) 3 procedures
4.1 measuring with a pH-meter 2

3. Determination of some inorganic and 4.2 chromatography on thin layers 3
organic compounds 4.3 column chromatography 3
- general principles 4.4 separation on ion exchanger 3
4.5. measuring of UV-VIS absorbances
3.1 quantitative determinations using with a spectral photometer 3
precipitation reactions 2 4.6. performing of conductivity
3.2 igniting of a precipitate in a crucible 1
3.3 quantitative volumetric measurements 3
determinations 1
3.4 rules at titrating 1 5. Evaluation of results
3.5 use of a pipetting ball 1
3.6 preparation of a standard solution 2 5.1 Estimation of experimental errors
3.7 alkalimetric and acidimetric (significant figures, plots scales) 1
determinations 2
3.8 color transitions of indicators at a
alkalimetric and acidimetric 6. If the organizer wants to apply a
determinations 2 technique which is not
3.9 direct and indirect determinations
mentioned in the above
(back titration) 3
3.10 manganometric determinations 3
syllabus, this technique is set to
3.11 iodometric determinations 3 level 3 automatically.
Mumbai, India, July 2001 xiii

Values of Some Fundamental Constants
Avogadro number NA = 6.022 x 1023 mol-1
Faraday constant F = 96485 C mol-1
Gas constant R = 8.314 J. K-1. mol-1
Planck’s constant h = 6.626 x 10-34 J.s
Mass of electron me = 9.110 x 10-31 kg
Notes:
1. The symbol [X] denotes concentration of X. It may carry the unit mol L-1 or, in
some places, may denote concentration relative to the standard concentration
of 1M, in which case it is dimensionless. The particular usage should be
obvious from the context. All equilibrium constants are dimensionless.
2. The knowledge of mathematics required for the contest problems of the 33rd
IChO will be no more than that indicated by the problems in this collection.
xiv
Theoretical Problems
Problem 1 Water
Water, the commonest substance around us, is an excellent system to understand

many concepts of thermodynamics. It exists in three different phases: solid (ice),
liquid and vapour. [At high pressures, different solid phases of ice exist, but we do
not consider them here.] The phase diagram for water, which gives the pressure
versus temperature curves for its different phases in equilibrium, is shown below:
A. Phase diagram
223
Pressure / bar
Solid Liquid
1.01
6.11 x 10−3
Vapour
0 0.01 100 374

Temperature / °C
Phase diagram of water (not to scale)
a. At what temperature and pressure do all the three phases of water coexist in
equilibrium?
b. What is the effect of decrease of pressure on boiling point of water and

melting point of ice, as seen from the phase diagram?
c. The liquid-vapour coexistence curve ends at the point Pc = 223 bar and Tc =
374oC. What is the significance of this point?
d. What is the phase of water at T = 300 K, P = 12.0 bar; T = 270 K, P = 1.00

bar?
Mumbai, India, July 2001 1

e. Below what value of pressure will ice, when heated isobarically, sublimate to
vapour?
f. At a certain temperature and pressure on the liquid-vapour co-existence line,

the molar volumes of water in the two phases are
Vl = 3.15 x 10 −5 m 3 V v = 15.8 × 10 −5 m3
For 1.00 mole of water in a 0.100 litre vessel at this temperature and
pressure, determine the volume fractions in liquid and vapour phases.
B. Clausius – Clapeyron equation
a. Explain your answer to part A. b above on the basis of the Clapeyron

equation.
b. Autoclaves used for medical sterilisation need to have a temperature of 120°C

of boiling water to kill most bacteria. Estimate the pressure required for the
purpose. The molar enthalpy change of vaporisation of water is 40.66 kJ mol−1
at the normal boiling point. Indicate the assumptions made in your estimate.
c. The molar enthalpy change of fusion at normal freezing point (273.15 K) is

6008 J mol−1. Estimate the pressure at which water and ice are in equilibrium
at – 0.200°C. Density of ice = 917 kg m −3 and density of water = 1000 kg m−3.
Indicate the assumptions made in your estimate.
C. Irreversible condensation
a. Consider 28.5 g of supercooled (liquid) water at −12.0°C and 1.00 bar. Does
this state lie on the P - T plane of the phase diagram?
b. This metastable state suddenly freezes to ice at the same temperature and
pressure. Treat the metastable state as an equilibrium state and calculate the
heat released in the process. Molar heat capacities, assumed constant, are :
C p(ice) = 76.1 JK −1mol −1

C p (liquid water) = 37.15 JK −1mol −1
∆H(fusion) = −333.5 J g −1
2 Mumbai, India, July 2001

c. Determine the total entropy change of the universe in the process and assure
yourself that the answer is consistent with the Second Law of
Thermodynamics. Take the surroundings to be at −12.0°C.
Problem 2 van der Waals gases
The ideal gas equation PV = nRT implies that the compressibility factor
PV
Z = = 1
nRT
However, the compressibility factor is known to deviate from 1 for real gases. In
order to account for the behavior of real gases, van der Waals proposed the
following equation of state :
 n 2a 
 P + 2  (V − nb ) = nRT
 V 
where a and b are constants, characteristic of the gas. The constant a is a measure
of the intermolecular force and b that of the size of the molecules.
a. Show on the basis of van der Waals equation that
i. at sufficiently high temperatures, Z is greater than unity for all

pressures. At high temperatures and low pressures, Z approaches the
value for an ideal gas.
ii. at lower temperatures, Z can be less than unity.
iii. for a = 0, Z increases linearly with pressure.
b. At a certain temperature, the variation of Z with P for He and N2 is shown

schematically in the following figure.
For He, a = 3.46 x 10−2 bar L2 mol−2 and b = 2.38 x 10−2 Lmol−1
For N2, a = 1.37 bar L2 mol−2 and b = 3.87 x 10−2 Lmol−1

1
2
Z=1
P →
Identify the graph corresponding to He and N2.
c. Two P-V isotherms of a van der Waals gas are shown below schematically.
Identify the one that corresponds to a temperature lower than the critical
temperature (Tc ) of the gas.
T1
P →
T2
V→
d. For a given P, the three roots of van der Waals equation in V coincide at a
certain temperature T = Tc. Determine Tc in terms of a and b, and use the
result to show that N2 is liquefied more readily than He.
e. Determine the work done by 1 mol of N2 gas when it expands reversibly and
isothermally at 300 K from 1.00 L to 10.0 L, treating it as a van der Waals gas.
Problem 3 Rates and reaction mechanisms
The observed rate law for a chemical reaction can arise from several different
mechanisms. For the reaction
H2 + I2 → 2 HI

the observed rate law is

d [H2 ]
− = k [H2 ] [I2 ]
dt
For a long time it was believed that the above reaction took place as it was written
down; that is, it was a bimolecular elementary reaction. It is now considered that
several mechanisms compete. Below a certain temperature, two alternative
mechanisms have been proposed :
(1) I2  2I K : equilibrium constant

I + I + H2 →
k1
2HI
(2) I2  (I2)d K' : equilibrium constant
(I2)d + H2 →
k1
2HI
where (I2)d represents a dissociative state of I2. The first step in each mechanism is
fast and the second slow.
a. Show that both mechanisms are consistent with the observed rate law.
b. The values of the rate constant k for the reaction at two different temperatures
are given in the table :
T(K) k (L mol−1 s−1)

373.15 8.74 × 10−15
473.15 9.53 × 10−10
i. Determine the activation energy Ea.

ii. The bond dissociation energy of I2 is 151 kJ mol−1. Justify why the
second step in each mechanism is rate determining.
c. The change in internal energy (∆U) for the reaction is − 8.2 kJ mol−1.
Determine the activation energy for the reverse reaction.
d. The activation energy for a reaction can even be negative. An example is the
gas phase recombination of iodine atoms in the presence of argon:
I + I + Ar → I2 + Ar ,

whose activation energy is about – 6 kJ mol−1.
One of the proposed mechanisms of this reaction is :
I + Ar + Ar  IAr + Ar K" : equilibrium constant
IAr + I →
k3
I2 + Ar
where IAr is a very loosely bound species.
i. Assume that the second step is rate determining and obtain the rate
law for the reaction.
ii. Give a possible explanation of why the activation energy for the iodine
recombination is negative.
Problem 4 Enzyme catalysis
Enzymes play a key role in many chemical reactions in living systems. Some
enzyme-catalysed reactions are described in a simple way by the Michaelis-Menten
mechanism, as given below.
k2
k1
E + S ES E + P
k1'
where E stands for the enzyme, S stands for the substrate on which it acts and P,
the end product of the reaction. k1 and k1' are the forward and backward rate
constants for the first step and k2 the forward rate constant for the second step.
Ignore the backward rate for the second step. Also assume that the enzyme
equilibrates with its substrate very quickly.
a. In an experiment, the initial rate (of formation of P) is determined for different

concentrations of the substrate, keeping the total concentration of enzyme fixed
at 1.5 x 10−9 M. The following graph is obtained.

3.0 x 10-6 M s−1
Initial rate → T = 285 K
1.5 x 10−6 M s−1
5.0 x 10−5 M
Substrate concentration [S] →
i. The graph is linear for small [S] and it approaches a constant value for
large [S]. Show that these features are consistent with the Michaelis-
Menten mechanism. (Use steady state approximation for the
intermediate step.)
ii. Determine the rate constant k2 for the second step.
iii. Predict the initial rate on the basis of the Michaelis-Menten mechanism
for the substrate concentration [S] = 1.0 x 10−4 M.
iv. Determine the equilibrium constant for the formation of the enzyme -
substrate complex ES.
b. The experiment above studied at 285 K is repeated for the same total enzyme
concentration at a different temperature (310 K), and a similar graph is
obtained, as shown below.

6.0 x 10−6 M s−1
Initial rate → T = 310 K
3.0 x 10−6 M s-1
8.0 x 10−5 M
Substrate concentration [S] →
Determine the activation energy for the conversion of ES to E and P.
c. One interesting application of the ideas above is the way enzyme catalysed
reactions inactivate antibiotics. The antibiotic penicillin is, for example,
inactivated by the enzyme penicillinase secreted by certain bacteria. This
enzyme has a single active site. Suppose, for simplicity, that the rate
constants obtained in a above apply to this reaction. Suppose further that a
dose of 3.0 µmol of the antibiotic triggers the release of 2.0 x 10−6 µmol of the
enzyme in a 1.00 mL bacterial suspension.
i. Determine the fraction of the enzyme that binds with the substrate
(penicillin) in the early stage of the reaction.
ii. Determine the time required to inactivate 50% of the antibiotic dose.
d. To control the inactivation of penicillin, suppose a substance is introduced

which has a similar structure to penicillin and is able to occupy the enzyme
site, but is otherwise completely unreactive. This naturally inhibits the
enzyme-catalysed reaction. The degree of inhibition i is defined by
r
i = 1−
r0
where r and r0 are the initial rates of reaction with and without the inhibitor
respectively.

Consider again the Michaelis-Menten type of mechanism to describe the

situation :
k1
E + S ES
k1'
k3
E + I EI
k3'
k2
ES E + P
i. Show that the degree of inhibition decreases with increase in

concentration of the substrate (for constant concentration of the
inhibitor), and the inhibitor ceases to be effective for large substrate
concentrations. (This is known as competitive inhibition.)
ii. For low substrate concentration of penicillin, determine the

concentration of the inhibitor that reduces the rate of the inactivation of
penicillin by a factor of 4. The dissociation constant of enzyme-inhibitor
complex is given to be 5.0 x 10−5.
Problem 5 Schrödinger equation
The simplest Schrödinger equation, describing a free particle confined to move in a

one-dimensional ‘rigid box’ brings out a most basic fact: quantization arises due to
boundary conditions on the wave function.
a. An electron of mass m is confined to move in a line along the x-axis from x = 0

to x = L. Between the two ends it experiences no force.
i. Write down the (time-independent) Schrödinger equation for the wave

function ψ of an electron.
ii. Which of the following are possible wave functions of an electron in
one-dimensional rigid box :
e− kx
nπx
cos
L
sin kx
nπx
sin
L
where k is any real number and n is a positive integer ?
iii. For the acceptable wave functions of the electron in (ii) above, show
that the energies are given by
h2 n2
En =
8 m L2
iv. Plot schematically the wave function of the electron in the ground and
the first two excited states. What is the number of nodes (in the region
between x = 0 to L) of the wave function with energy En?
v. Normalize the ground state wave function of the electron.
(The integral of the square of the modulus of a normalized wave
function over all space is unity.)
b. An interesting example of this one-dimensional model in chemistry is the

motion of an electron in a conjugated system of single and double bonds. The
molecule 1,3-butadiene has four π electrons assumed to move freely in a line
consisting of three carbon-carbon bonds, each of approximately the same
length (1.4 × 10−10 m), with an additional length of 1.4 × 10−10 m at each end.
Using the aufbau principle, determine a scheme to fill the electrons in the
available energy levels. Calculate the lowest excitation energy of the system.
c. ‘Boundary conditions’ on wave functions result in quantization of not only
energy but also other physical quantities, such as angular momentum.
The wave function corresponding to the value hλ/2π for the z-component of
angular momentum (Lz) is:
iλφ
ψ(φ) = e ,
where φ is the (azimuthal) angle in the x-y plane measured relative to the x-
axis. Use the condition that this function is single valued at every point in
space and show that this implies that λ is quantized. Give the quantized
values of angular momentum projection along the z-axis.

Problem 6 Atomic and molecular orbitals
Orbitals are one-electron wave functions, whether they refer to electronic motion in
an atom (atomic orbitals) or in a molecule (molecular orbitals) or a solid. Each orbital
corresponds to a certain probability distribution of finding an electron in different
regions of space.
A. Atomic orbitals
a. The 1s orbital of hydrogen atom is given by
− r/ao
ψ =e ,
1s
where ao is the Bohr radius (ao = 5.3 × 10−11 m) and r is the radial co-
ordinate (distance of a point in space from the centre).
i. Normalize the given wave function.
ii. At what distance from the nucleus is the electron most likely to be
found?
b. The wave functions for 2s, 2pz and 3dz2 states are given below :
r
−
r
ψ2s = (2 − ) e 2ao
ao
r
 r  −
ψ2p z =   cos θ e
2a o
a 
 o
r
−
 r2  3a o
ψ =  2  (3 cos2θ − 1) e
3d 2
z  ao 
What are the nodal surfaces of these orbitals?
c. It turns out that the solution of Schrödinger equation for a one-electron atom
yields exactly the ‘good old’ formula of Bohr for quantized energies:
(13.6 eV)Z 2
En = −
n2
where, for convenience, the numerical value of the combination of constants
appearing in the formula has been put in units of eV .

It is fun using this formula for a neutral helium atom, but we must exercise
some care. In a helium atom, each electron ‘sees’ the nucleus screened by
the other electron. That is, the effective charge of the nucleus ‘seen’ by each
electron decreases from its bare value Z=2 to some other value, say, Zeff . The
ionization energy for a helium atom in its ground state is known
experimentally to be 24.46 eV. Estimate Zeff .
B. Molecular orbitals
Molecular orbitals of a hydrogen molecule ion (H2+) can be approximately written as

linear combinations of atomic orbitals centered around the two nuclei of the
molecule. Consider the (unnormalized) molecular orbitals constructed in this manner
from the 1s and 2s orbitals of two hydrogen atoms, say, A and B:
ψ1 = ψ1s + ψ1s
A B
~ = ψA − ψB
ψ1 1s 1s
ψ2 = ψ2s
A
+ ψB2s
~ = ψA − ψB
ψ 2 2s 2s
Taking the z-axis along the line joining the two nuclei, the orbital contours of ψ1 and
ψ1 are shown schematically below :
Similar orbital contours (curves on which the value of ψ is constant) can be drawn for
ψ2 and ψ2 .
The energies of these wave functions as a function of internuclear distance are

shown below schematically:

~
Ψ2
Ψ2
E/eV−3.4
~
Ψ1
Ψ1
−13.6
−15.6
1.32
R/10−10
a. →
Identify the bonding and antibonding orbitals. State qualitatively what
makes one orbital bonding and another antibonding.
b. Determine the values of the equilibrium internuclear distance Re and the

dissociation energy D of the ground state of H2+.
c. If the molecular ion H2+ is excited to the state ψ2, to what atomic states will it
dissociate?
In the following questions, assume that the energy versus internuclear distance
graphs for the orbitals of H2 and He2 are similar to the one shown for H2+.
d. Explain why the ground state total electron spin of the neutral H2 molecule is
zero.
e. Write down the electronic configuration of the first excited state of H2

molecule. Predict if it will stay bound or dissociate.
f. It is difficult to obtain He2 in its ground state, but it has been observed in its
excited states. Explain how this is possible.
Problem 7 Fission
a. Consider the following fission reactions of 235U by thermal neutrons :
235
92 U + n → 94
38 Sr + 140
(...) Xe + (.....)
235
92 U + n → 141
56 Ba + (....) + 3n

Identify the missing species and numbers.
b. Consider the first of the reactions above. The unstable fission fragments
undergo successive β-decays giving Zr and Ce. Write down the net nuclear
reaction and calculate the total energy released in MeV. You are given the
following data on atomic masses :
m ( 235 U) = 235.0493 u
m ( 94 Zr) = 93.9063 u
m (140 Ce) = 139.9054 u
mn = 1.00866 u
1u = 931.5 MeV/c 2
c. 1 kg of natural uranium metal was put in a nuclear research reactor. When the
total energy released reached 1 Mega Watt Day (MWd), it was removed from
235
the reactor. What would be the percentage abundance of U in the uranium
metal at that time, if it is 0.72% in natural uranium. Your result in b. above may
be taken to be the average energy released per fission. Assume that all the
energy is due to fission of 235U only.
Problem 8 Radioactive decay
The radioactive isotope 210

Bi is the daughter product of 210
Pb and decays by β -
emission to 210Po, which is also radioactive. 210Po decays by α-emission to the stable
206
Pb.
210 β 210 β 210 α 206

Pb Bi Po Pb
T1/2 = 22.3 y T1/2 = 5.01 d T1/2= 138.4 d
210 210
A sample of radiochemically pure Bi was freshly isolated from Pb and was
210 210
allowed to stand for the growth of Po. The radioactivity of the freshly purified Bi
sample was 100 µCi. (1 Ci = 3.7 x 1010 disintegration per second)
a. What is the initial mass of the sample (210Bi)?
210
b. Calculate the time it takes for the amount of Po in the sample to grow to its
maximum value. How much is the maximum amount of 210Po?

c. Determine the α-disintegration rate of 210

Po and β-disintegration rate of 210
Bi
at that time.
Problem 9 Redox reactions
a. A solution containing Sn2+ ions is titrated potentiometrically with Fe3+. The

standard reduction potentials for Sn4+/2+ and Fe 3+/2+ are given below.
Sn4+ + 2e-  Sn2+ E° = 0.154 V
Fe3+ + e-  Fe2+ E° = 0.771 V
i. Write down the overall reaction and calculate the standard free energy
change of the overall reaction.
ii. Determine the equilibrium constant of the reaction.
b. If 20 mL of 0.10 M Sn2+ is titrated with 0.20 M Fe3+ solution, calculate the

voltage of the cell
i. when 5 mL of Fe3+ solution is added.
ii. at the equivalence point.
iii. when 30 mL Fe3+ of the solution is added.
The saturated calomel electrode (E° S.C.E = 0.242 V) is used as the reference
electrode in the titration.
c. One of the important analytical methods for estimation of Cu2+ is iodometric

titration. In this reaction Cu2+ is reduced to Cu+ by I− and the liberated I2 is
then titrated with standard Na2S2O3 solution. The redox reaction is as follows:
2Cu2+ + 4I− → 2CuI(s) + I2 (aq)
Electrode potentials of the relevant half-cells are:
Cu2+ + e-  Cu+ E° = 0.153 V
I2 + 2e-  2I− E° = 0.535 V

A consideration of the electrode potentials would indicate that reduction of Cu2+ by I−

is not a spontaneous reaction. However, in the iodometric titration this reaction does
take place. Let us try to understand the anomaly:
i. CuI has low solubility in water with Ksp ≈ 1.1× 10−12. Calculate the
effective E° value for the equilibrium CuI(s)  Cu+ + I−.
ii. Using the result in i., calculate the effective E° value for the reduction
of Cu2+ by I−. What does this value suggest about the spontaneity of
the reaction?
iii. Calculate the equilibrium constant of the reduction reaction in ii.
Problem 10 Solubility of sparingly soluble salts
Two important factors that affect the solubility of a sparingly soluble salt are pH and
the presence of a complexing agent. Silver oxalate is one such salt, which has low
solubility in water (2.06 x 10−4 at pH = 7.0). Its solubility is affected by pH as the
anion oxalate reacts with hydronium ions, and also by a complexing agent such as
ammonia as the cation silver forms complexes with ammonia.
a. Calculate the solubility of silver oxalate in acidified water with pH = 5.0. The
first and second dissociation constants for oxalic acid are 5.6 x 10−2 and 6.2 x
10−5 respectively.
b. In the presence of ammonia in aqueous solution, silver ion forms two
complexes Ag(NH3)+ and Ag(NH3)2+. The values of the stepwise stability
constants for the formation of these complexes are 1.59 x 103 and 6.76 x 103.
What is the solubility of silver oxalate in an aqueous solution that contains
0.02 M NH3 and has pH = 10.8?
Problem 11 Spectrophotometry
a. Manganese and chromium in steel can be determined simultaneously by

absorption spectral method. Dichromate and permanganate ions in 1M H2SO4
(Cr2O72− and MnO4−) absorb at 440nm and 545nm. At these wavelengths,
molar absorptivity of MnO4− is 95 Lmol−1cm−1 and 2350 Lmol−1cm−1
respectively and that of Cr2O72− is 370 Lmol−1cm−1 and 11 Lmol−1cm−1
respectively.

A steel sample, weighing 1.374g was dissolved and Mn and Cr in the resulting
solution oxidised to MnO4− and Cr2O72−. The solution was diluted with 1M
H2SO4 to 100.0mL in a volumetric flask. The transmittances of this solution
were measured with a cell of 1.0cm path length and with 1.0M H2SO4 as
blank. The observed transmittances at 440nm and 545nm respectively were
35.5% and 16.6%.
Calculate from these data the percentage of Mn and Cr in the steel sample.
Assume that Beer’s law is valid for each ion and that the absorption due to
one ion is unaffected by the presence of the other ion .
b. Cobalt (II) forms a single complex CoL32+ with an organic ligand L and the
complex absorbs strongly at 560nm. Neither Co(II) nor ligand L absorbs at
this wavelength. Two solutions with the following compositions were prepared:
Solution 1 [Co(II)] = 8 x 10−5 and [L] = 2 x 10 −5 .
Solution 2 [Co(II)] = 3 x 10−5 and [L] = 7 x 10 −5 .
The absorbances of solution 1 and solution 2 at 560nm, measured with a cell

of 1.0cm path length, were 0.203 and 0.680 respectively. It may be assumed
that in solution 1, all the ligand is consumed in the formation of the complex.
From these data calculate the
i. molar absorptivity of the complex CoL32+
ii. stability constant for the formation of the complex CoL32+.
Problem 12 Reactions in buffer medium
An organic nitro-compound (RNO2) is electrolytically reduced in an aqueous acetate

buffer solution having total acetate concentration (HOAc + OAc−) 0.500 and pH = 5.0.
300 mL of the buffered solution containing 0.01M RNO2 was reduced completely. The
dissociation constant for acetic acid is 1.75 x 10−5 at 25 °C. The reduction reaction is
RNO2 + 4H+ + 4e- RNHOH + H2O
Calculate the pH of the solution on completion of the reduction of RNO2.

Problem 13 Identification of an inorganic compound
Some observations related to an unknown inorganic substance A are presented

below.
♦ A is a yellowish – white deliquescent solid and it sublimes on heating. It has a

molecular weight of 266.
♦ A reacts violently with water, forming solution B.
♦ When a solution of NH4Cl and NH4OH is added to solution B, a white gelatinous

precipitate is obtained.
♦ A sample of B also gives a curdy white precipitate C on addition of dilute nitric

acid and silver nitrate solution. This white precipitate C readily dissolves when
dilute NH4OH is added, though a gelatinous white precipitate D is formed in its
place with excess NH4OH.
♦ Precipitate D is filtered off and is dissolved in excess NaOH to give a clear

solution E.
♦ When CO2 is passed through solution E, compound D is reprecipitated.
♦ Substance A dissolves unchanged in dry ether. When this solution is reacted with
LiH, a product F is formed. If LiH is used in excess, F transforms to G.
a. Identify the unknown compound A.
b. Write down the appropriate chemical equations for the given reactions and
identify the different products from B to G.
Problem 14 Ionic and metallic structures
Modern methods of structural analysis using X-rays provide valuable information

about the three dimensional arrangement of atoms, molecules or ions in a given
crystal structure.

a. Crystal structure of rock salt (NaCl) is given below.
i. What is the type of crystal lattice presented in the diagram?
ii. What is the coordination number of a sodium ion in this structure?
iii. What is the number of formula units of NaCl per unit cell?
iv. Calculate the r+ / r− limiting radius ratio for this type of structure.
v. Why is the array of chloride ions slightly expanded, with the nearest
Cl-Cl distance being 400pm, compared to the close packed value of
362 pm?
vi. What happens when the cation radius in the structure shown above is
progressively increased till the cation/anion radius ratio reaches a
value of 0.732?
vii. What is the range of cation/anion radius ratio for which the structure
like that of NaCl is stable?
b. The Cu - Kα X-ray(λ = 154pm) reflection from (200) planes of sodium chloride

crystal is observed at 15.8°. Given that the radius of the chloride ion is 181
pm, calculate
i. the separation between adjacent 200 planes of NaCl.
ii. the length of the unit cell edge (lattice constant) of NaCl.
iii. the radius of the sodium ion.

c. The diagram of a cubic close packing (ccp) and a hexagonal close packing (hcp)
lattice arrangement (assuming rigid sphere model) is given below.
i. Describe the difference between the ccp and hcp lattice arrangements.
ii. Calculate the packing fraction for a ccp arrangement.
iii. Will the coordination number and the packing fraction in a hcp
arrangement be the same as that in a ccp arrangement?
d. Nickel (at.wt. 58.69) crystallizes in the ccp structure. X-ray diffraction studies
indicate that its unit cell edge length is 352.4 pm. Given that the density of
Nickel is 8.902 g cm-3, calculate
i. the radius of the nickel atom.
ii. the volume of the unit cell.
iii. the Avogadro number.
Problem 15 Compounds of nitrogen
a. Nitrogen forms a number of oxides. One of the important oxides of nitrogen is

NO2, a red-brown colored reactive gas.

i. Draw the Lewis structure of NO2 and predict its shape using valence
shell electron pair repulsion theory.
ii. Using VSEPR, predict the shapes of the NO2− and NO2+ ions. Compare
the shapes of these two ions with that of NO2 .
b. Consider two other compounds of nitrogen, trimethylamine (Me3N) and

trisilylamine (H3Si)3N. The observed bond angles at nitrogen in these
compounds are 108° and 120° respectively. Explain the difference in the bond
angles.
c. Both nitrogen and boron form trifluorides. The bond energy in BF3 is 646
kJ/mole and that in NF3 is only 280 kJ/mole. Account for the difference in
bond energies.
d. The boiling point of NF3 is –129°C while that of NH3 is –33°C. Ammonia acts
as a Lewis base whereas NF3 does not. The observed dipole moment of NF3
(0.24 D) is much less than that of NH3 (1.46 D), even though fluorine is much
more electronegative than hydrogen.
i. Explain the differences between boiling points and basicities of NF3

and NH3.
ii. Account for the low dipole moment of NF3.
e. The reaction of aqueous sodium nitrate with sodium amalgam as well as that
of ethyl nitrite with hydroxylamine in presence of sodium ethoxide give the
same product. This product is the salt of a weak unstable acid of nitrogen.
Identify the acid and write down its structure. This acid isomerises into a
product, which finds use in propellant formulations. Write the structure of the
isomer.
Problem 16 Structure elucidation with stereochemistry
Citric acid (2-hydroxy-1,2,3-propanetricarboxylic acid) is the primary acid of citrus

fruits, which contributes to their sour taste. Commercial manufacturing of citric acid
involves fermentation of molasses or starch using the fungus Aspergillus niger at pH

3.5. It is widely used in food, soft drinks and as a mordant in dyeing. It is also an
important biochemical intermediate.
a. What transformation will citric acid undergo when warmed with concentrated sulfuric
acid at 45-50°C? Give the structure and IUPAC name of the product obtained.
Which type of organic acids would undergo a similar reaction?
After warming citric acid with sulfuric acid, anisole (methoxybenzene) is added to the
reaction mixture and product A (C12H12O5) is obtained.
On heating with acetic anhydride, A forms an anhydride.
118 mg of A requires 20 mL of 0.05 N KOH for neutralisation.
Reaction with bromine indicates that the same amount of compound A requires
80 mg of bromine to give an addition product.
b. Deduce the structure of A.
c. Identify the possible isomers of A in this reaction and give their structures,
absolute configurations and the IUPAC names.
d. In the bromination reaction, how many stereoisomers of A will be obtained? Draw

their Fischer projections.
e. Assign absolute configurations to the stereocentres in all the stereoisomers formed

in d.
Instead of anisole, if phenol and resorcinol are separately added to the reaction
mixture, compounds B and C are obtained, respectively. B does not give any
coloration with neutral FeCl3, but C does. Under identical reaction conditions, the
yield of compound C is much higher than that of B.
f. Give appropriate structures for B and C.
g. What is the difference between the reactions leading to the formation of A and B?
h. Why is the yield of C higher than that of B?

Problem 17 Organic spectroscopy and structure determination
The following observations were recorded for identifying two compounds A and B.
1
Both have the molecular formula C3H6O. Schematic H-NMR spectra of these
compounds at 400 MHz are presented in the following figure. The peak positions and
the relative intensities of the different lines in the 1H-NMR spectrum of B are given in
the accompanying Table (Note: the values have been altered slightly from the
experimental values to facilitate analysis.)
One of these compounds reacts with malonic acid to form a compound known as
Meldrum's acid, with the molecular formula C6H8O4 which gives peaks between 0 and
7.0 δ in its 1H-NMR spectrum. The IR spectrum shows a peak in the region 1700 - 1800
cm-1. It condenses with an aromatic aldehyde in the presence of a base.
7 6 5 4 3 2 1 0
chemical shift (δ)
1
H-NMR schematic spectra of A and B at 400 MHz

1
Peak positions and relative intensities of individual lines in the H NMR
spectrum (400 MHz) of B
Line (ppm) Relative Line (ppm) Relative

intensity intensity
1 6.535 1 8 3.870 1
2 6.505 1 9 3.525 1
3 6.495 1 10 3.505 1
4 6.465 1 11 3.495 1
5 3.930 1 12 3.475 1
6 3.910 1 13 3.000 12
7 3.890 1
a. Label the unknown compounds in the bottles with IUPAC names, using the NMR
spectra given in the figure.
b. In the 1H-NMR spectrum of B, assign the peak positions to specific protons.
c. Calculate the spin-spin coupling constants for protons of compound B.
d. Convert the peak positions of the first four lines into Hz (refer to theTable). What
will be the peak positions of these lines in Hz, if the spectrum is recorded on
a 600 MHz instrument?
e. Draw the possible structure of Meldrum's acid.
f. Meldrum's acid has pKa = 4.83. Explain the acidity of Meldrum’s acid.
g. Give the structure of the condensation product of Meldrum's acid with an

aromatic aldehyde.

Problem 18 Polymer synthesis
Ethylene finds extensive application in the manufacture of polymers and bulk

chemicals. It is produced on a large scale by thermal and catalytic cracking of
alkanes obtained from natural gas and petroleum.
In the presence of silver catalyst, ethylene reacts with oxygen to give P. Compound
P on heating with acidified water forms Q. 1H-NMR spectrum of P has only one
signal while that of Q contains two signals.
a. Identify and draw the structures for compounds P and Q.
Compound R is obtained when P and Q react with each other. R reacts with SOCl2
to give S. On heating with alcoholic KOH, S gives T, an anaesthetic under the name
"vinethene".
SOCl2 alc.KOH
P + Q R S T
b. Identify the compounds R, S and T.
Another compound dimethyl benzene-1,4-bis(acetate) can be synthesised from

p-xylene. Such a synthesis requires use of proper reagents so that desired
intermediate compounds and the final product are obtained. Various intermediate
compounds obtained in the synthesis of dimethyl benzene-1,4-bis(acetate) along
with their structures are shown below.
COOH COOCH3
CH3 CH2CN CH2 CH2

CH2Br
? ? ? ?
? ? ? ?
CH3 CH2CN CH2 CH2

CH2Br
p-xylene COOH COOCH3

Dimethyl benzene -1,4 -
bisacetate
c. Identify the reagents used in this synthesis of dimethyl benzene –1,4-

bis(acetate).

d. How many peaks would you expect in the 1H-NMR spectrum of dimethyl
benzene –1,4-bis(acetate)?
When dimethyl benzene-1,4-bis(acetate) (synthesised from p-xylene) and compound

R (obtained from ethylene) are heated together a polymer is formed.
e. Draw the structure of the polymer.
f. What happens when this polymer is treated with
aq KOH (heat), then H+ / H2O?
LiAlH4?
g. Inadvertently, an excess of dimethyl benzene-1,4-bis(acetate) was heated

with glycerol and a different polymer was obtained. What is the likely structure
of this polymer? Will it be suitable for drawing fibres?
Problem 19 Organic synthesis involving regioselection
One crucial problem in organic synthesis concerns the synthesis of a specific

disubstituted benzene through an electrophilic substitution reaction on a
monosubstituted benzene. This problem is elegantly tackled in the synthesis of
Tramadol, an analgesic drug (C16H25NO2), described below. The first step in this
synthesis invovles :
HSbF6
Phenol A
halogen
A gives two equal intensity peaks at 172 and 174 in the highest m/z region of its
mass spectrum. It gives a mixture of three isomeric mononitro derivatives on nitration
under mild conditions.
a. Draw the structure for compound A. What is the regioselection observed in

the reaction of phenol to form A? State the significance of this reaction.

Consider the following reaction
( CH3 )2SO4 / NaOH Mg / THF / toluene

A B C
Mass spectrum of B shows equal intensity peaks at 186 and 188 in the highest m/z
region.
b. Give structures of compounds B and C. How does the reactivity of B change on

its conversion to C?
Another intermediate compound D required for the synthesis of Tramadol is obtained

as follows
paraformaldehyde
Cyclohexanone dimethylamine
D ( C H NO )
9 17
( Dissolves in HCl )
hydrolysis
C + D [E] Tramadol
c. Show the structures of compound D and the final product Tramadol.
d. Give the structures of the possible stereoisomers of Tramadol.
Problem 20 Carbon acids
Keto esters are bifunctional reactive molecules and are important synthons for the
synthesis of aliphatic and heterocyclic compounds.
a. Two isomeric keto esters X and Y have the same molecular formula C5H8O3.
Deduce their possible structures.
Each ester is first reacted with benzyl bromide in the presence of CH3ONa, and the
resulting products are treated with 1 or 2 equivalent of a strong base (such as lithium
diisopropyl amide, LDA) followed by 1 equivalent of CH3I.
The products at the end of the second step are then hydrolysed by aq.HCl.
b. Write down the reaction sequences involved.

c. At the end of the reaction, the final product of keto ester X is a neutral
compound (molecular formula C11H14O) whereas keto ester Y gives a keto
acid (molecular formula C12H14O3). Explain.
d. Keto ester X gives different products depending upon the amount of LDA used.
Explain what happens when
i. 1 equivalent of LDA is used.
ii. 2 equivalents of LDA are used.
Problem 21 Amino acids and enzymes
Amino acids are the building blocks of proteins. The presence of –NH2 and -COOH
groups makes amino acids amphoteric in nature. Certain amino acid side chains in
proteins are critically important for their reactivity and catalytic role. Glutamic acid is
one such amino acid, whose structure is shown below.
-
COO ( pKa = 2.2 )
+
( pKa = 9.7 ) H3N CH
CH2
CH2
-
COO ( pKa = 4.3 )
a. Why is the pKa of the α-COOH group lower than that of the γ-COOH ?
b. Calculate the percent of γ-COOH group that remains unionized at pH 6.3.
c. Glutamic acid is subjected to paper electrophoresis at pH = 3.25. Will it move

towards the anode (+) or cathode (-) ? Why ?
Hydrolysis of polysaccharides like chitin, cellulose and peptidoglycan is a common

biochemical process. This involves the hydrolysis of a glycosidic bond like the β-1, 4
linkage shown below.

O
B O
A O
C1 C4 O
β-1, 4 linkage
One such hydrolysis reaction is catalysed by lysozyme.
18
d. Suppose the lysozyme catalyzed reaction is performed in O enriched water.
18
Do you expect the O to be incorporated into the product? If yes, where?
The pH-activity profile of lysozyme is shown in the figure
Relative Activity
(%)
3 5 7
pH
e. Explain this pH behavior in terms of two carboxylates (Asp-52 and Glu-35)

present at the lysozyme active site (note : ionizable groups on the substrate are
not involved). Write the ideal state of ionization at the lysozyme active site at
pH 5.0.
f. The pKa of Glu-35 in lysozyme active site is 6.0 and not 4.3 as found in the free
amino acid. Which of the following local effects is likely to be involved?
1. Enhanced negative charge

2. Enhanced positive charge
3. Enhanced polarity
4. Diminished polarity
Organic model reactions have helped to understand many features of enzyme

catalytic mechanisms. When a reaction is made intramolecular (like the enzyme
catalysts do!), rate acceleration takes place as if the apparent reactant concentration
felt at the site is enormously raised. The carboxylate group assisted hydrolysis of
three phenylacetates and their rate constants (k) are shown below.
O
(1) -1
H3 C C O k1 = 0.002 s
-
(when [ CH COO ] =1 M )
+ 3
-
H3 C COO (pseudo first order)
(2) O
k2 = 0.4 s -1
C O
-
COO (first order)
O
(3)
C O -1
k3 = 20 s
- (first order)
COO
g. Calculate the effective local concentration of the COO- group felt in (2) and (3)
above.
h. Why do you see a higher rate in (3) than in (2) ?

Problem 22 Coenzyme chemistry
The protective outer cell wall in bacteria has D-alanine as one of the building blocks.
However, metabolically only L-amino acids are available. Bacteria make D-alanine by
inverting the L-alanine. The structure of L-alanine is given below :
H
Me COOH
NH2
L-alanine
The abstraction of α-proton from L-alanine and reprotonation of the resultant

carbanion from the opposite side appears to be a simple process. However, it is not
easy to deprotonate alanine unless its NH2 group is masked and Cα-H is activated as
an acid.
Both these steps are brought about by the coenzyme pyridoxal phosphate (PLP) in
the presence of the enzyme alanine racemase. The following observations made in
certain model reactions will help you appreciate the role of PLP as the coenzyme.
Under favorable experimental conditions, benzaldehyde can be used as a reagent to

racemize alanine. In other words, it can mask the amine group and activate the Cα-
H of alanine making it more acidic.
CHO
L-alanine D / L-alanine
Base
a. Propose a stepwise mechanism for this base catalyzed racemisation of L-alanine

involving benzaldehyde as the reagent.
Compared to benzaldehyde, PLP is a somewhat complex molecule. With the help of

a few carefully designed aromatic aldehydes, good insight about the role of PLP as a
coenzyme can be obtained.
A few relevant structures are presented below. Underneath each, there is an

indication about its activity.

CHO CHO
O
- OH
O P O HO OH
OH +N Me
H +N Me
H
P LP (1 )
A ctive Pyridoxal (2)
Active
CHO
H3C OH CHO
OCH3
O
+N Me
H +N Me
H
(3)
Active (4)
Inactive
CHO
OH CHO
HO
OH
HO
NO2
O2N NO2
(5)
(6)
Active
Inactive
b. Based on this information, what inferences can you draw about the structural
requirements for PLP to act as a coenzyme?
c. A trivalent metal ion is actually critically needed for any of the above shown
compounds to display PLP-like activity without the involvement of the enzyme.
Suggest a plausible explanation for the role of the metal ion.
d. PLP is quite a versatile coenzyme. It participates in a variety of biologically

important reactions. The activity of PLP is due to its functioning as an electron
sink that stabilizes carbanions.
An important illustration of catalytic versatility of PLP is in the biosynthesis of the

neurotransmitter gamma amino butyric acid (GABA). As shown below, GABA is
made in a single step from L-glutamic acid. Suggest a mechanism explaining the role
of PLP as the coenzyme in this particular reaction.
- -
OOC COO - OOC
PLP + CO2
+ NH + NH
3 3
Glutamic Acid GABA

e. In yet another PLP mediated reaction, L-serine serves as a one-carbon donor

in a complex process of nucleotide biosynthesis. The enzyme serine
hydroxymethyltransferase degrades L-serine with the help of PLP into the
simpler amino acid glycine. An important metabolic intermediate (X) is
obtained as the side product in this reaction. Identify the one carbon metabolic
intermediate formed by analyzing its PLP based mechanism.
- -
COO COO
HO PLP
+NH + (X)
+NH
3 3
L-Serine Glycine
Problem 23 Protein folding
The link between amino acid sequence of a protein (the primary structure) and its
precise three-dimensional fold (the tertiary structure) remains one of the most
important unsolved mysteries of modern science.
All protein backbones are identical: planar amide units are linked via tetrahedral
methylene bridges, the so called α-carbons. Each α-carbon carries an R group of a
specific α-amino acid (see the following diagram).
A unique sequence of amino acids characterizes a particular protein, determining

how it folds and functions.
a. Every amide group in the polypeptide backbone, including its flanking α-

carbons, is a planar unit. Explain.
b. The α-carbons across each amide unit occur in a trans geometrical

arrangement. However, in case of the amino acid proline, both cis and trans
amide arrangements are almost equally favored. Why?

c. The conformational choices of amino acid residues in a polypeptide chain are

stereochemically controlled. For nineteen of the genetically coded amino
acids, the conformational choice is largely restricted to the α (folded) and β
(extended) regions of the Ramachandran diagram. For the amino acid
glycine, however, the conformational choices are much wider. Explain.
d. When a linear polypeptide folds forming a globular protein, an amino acid

residue may assume α or β conformation. However it is observed that
consecutive residues generally assume α or β conformation, rather than a
random combination of α and β. Explain.
e. In an aqueous environment polypeptides generally fold into compact globular

protein structures. The reason is (select one) :
1. The R groups in polypeptides are largely polar.

2. The R groups in polypeptides are largely nonpolar.
3. Both polar and nonpolar R groups occur in comparable proportion.
Justify your answer.
f. The pattern of R group polarities has an important role in determining whether

α-helix or β-sheet will form when a polypeptide folds in water at an apolar
surface. Explain the role of R group polarities.
Problem 24 Protein sequencing
Sequencing of a protein (polypeptide) involves the following steps: a) purification, (b)

determination of N-terminal amino acid, (c) cleavage of the polypeptide chain by
chemical or enzymatic methods, (d) isolation of the peptide fragments and (e)
determination of their sequence by an automated sequencing machine (sequenator).
It is also possible to sequence the mixture of peptide fragments without resolving it.
The final sequence can be determined by constructing overlapping sequences after

analyzing the information on the positional data on amino acids in different
fragments.
A small protein made up of 40 amino acid residues was sequenced as follows :

• Edman degradation involves treatment with phenyl isothiocyanate, subsequent

hydrolysis and spectrophotometric identification of the modified amino acid. This
procedure identified aspartic acid (Asp) as the N-terminal residue.
• The protein was cleaved with CNBr (cyanogen bromide) which cleaves the
peptide bond between methionine and any other amino acid on its C-terminal
side. The resulting peptide fragments were not separated. This mixture of
peptides was analyzed on the protein sequenator. Therefore, the sequenator
would detect as many amino acids in the given position as the number of
fragments. The results are shown in Table 1(a).
• The protein was digested with a proteolytic enzyme trypsin. This enzyme cleaves
the peptide bond between a basic amino acid (Arg or Lys) and the next C-
terminal residue. The resulting mixture of peptides was also analyzed as above.
The results are shown in Table 1(b).
Given this information:
a. Deduce the amino acid sequence common to the first fragment (N-terminal)
obtained by CNBr and trypsin treatments.
b. Deduce the sequence of the first fragment generated by CNBr treatment.
c. Deduce the entire sequence in the original polypeptide. Indicate the CNBr-
labile and trypsin-labile sites in this sequence.
d. What percentage of the total residues are basic amino acids?
e. If the polypeptide were to exist as an α helix, what will be the length of this α
helical structure?

Table 1. Data from protein sequenator .
Position number
Treatment 1 2 3 4 5 6 7 8
a) CNBr: Arg Gln Asn Arg Asn Arg Ala Ala
Asp Pro Pro His Ilu His Gly Lys
(Met) Glu Thr Ser Ilu Leu Trp Phe Met
Gly Tyr Tyr Val Phe Val Thr Tyr
b) Trypsin: Asp Cys His Ala Ilu Arg Cys Glu

Gly His Met Asn Leu Phe Lys Leu
(Arg or Lys) Gly Pro Thr Glu Thr Ser Ilu
Phe Pro Tyr Val Trp Ser
Tyr Tyr
f. What will be the size of the DNA segment (exon) coding for this polypeptide of
40 amino acids? Give the size in base pairs as well as in daltons. (consider
average molecular weight of a nucleotide in DNA = 330).
g. Assuming that the DNA corresponding to the exon contains equal numbers of
Adenine and Cytosine, calculate the number of H-bonds which will hold this
double helix.

Practical Problems
Safety Regulations
The following regulations apply to all laboratories used for the Olympiad. Participating
students must be well acquainted with these regulations and should study them
seriously. These rules will be strictly followed in the 33rd IChO practical examination.
Students who break any of these rules will be given only one warning before they are
disqualified from the practical examination.
If any questions arise concerning safety procedures during the practical examination,
students should not hesitate to ask the nearest instructor for directions.
All students are required to sign a statement agreeing that they have read and
understood the rules prior to the examination.
Rules for personal safety
a. For eye protection, safety goggles must be worn in the laboratories at all times. If
the student wears contact lenses, full protection goggles, which provide total seal
around eyes, must be worn. All students are requested to bring their safety
goggles, but we shall have some in reserve.
b. A long sleeved, knee length laboratory coat is recommended. Long pants and
closed-toed shoes must be worn for individual safety. Loose clothing, open style
shoes and sandals are prohibited. Long hair must be contained. Each student
will have to get her/his own necessary items for herself/himself.
c. Prior to the examination, the demonstrator-in-charge will check all protective

equipments to ensure that they are in order.
d. Pipetting by mouth is strictly forbidden.
e. Eating, drinking or smoking in the laboratory is strictly prohibited.

Accidents and first aid
In any chemistry laboratory, accidents can take place due to spillage of chemicals,
broken glasswares and fire. Any injury, illness, or incident, however minor, must be
reported to the instructor immediately so that proper corrective action can be taken up.
a. Chemicals: Every chemical in the laboratory must be handled with utmost care.
Chemicals can be corrosive, flammable or poisonous. Each student should read
the safety notes related to the chemicals given in the task before handling them.
The following general precautions must be always followed in the laboratory :
♦ Chemicals should never be tasted. Use pipette bulbs or pipette fillers all the
time.
♦ Spillage on the skin: For any spillage of chemicals, the first step is to flush
the skin under cold tap water for 10 to 15 minutes and then seek first aid/or
medical help as appropriate. Organic materials tend to get absorbed on the
skin, so wash the skin with warm water and soap, after cleaning it with cold
water. Contaminated clothing should be removed at the earliest.
♦ Chemicals in the eye: The proper use of safety goggles will reduce the risk of
any eye injury. Even so, if there is any splash of chemicals into the eyes,
wash your eyes with cold water for 15 minutes and then look for appropriate
medical attention.
b. Fire: Many chemicals are flammable, and hence no open flames are permitted
when such chemicals are in use. You should get familiar with the location of the
nearest fire extinguisher and fire blanket.
c. Glassware: Glass is a very hard but brittle material, and can break under stress
or strain. Please handle the glasswares very carefully. If breakage occurs it is
essential that any particles or splinters, specially from the wounds, are removed
at the earliest. The injuries must be inspected by the demonstrator-in-charge.

Please report and clean up any breakage of the glassware. Necessary

replacements can be obtained from the instructor.
d. Waste Materials: Do not dispose of chemicals in the sink. Please follow all
disposal rules provided in the task notes. Waste collection containers will be
provided wherever necessary.
e. Care of Benches and Apparatus: Each student is responsible for her/his section
of the bench. Any spillage of chemicals or water must be wiped immediately.
Concentrated acid spills must be first neutralized with sodium bicarbonate and
then washed with plenty of water. Your working area must be kept clean at all
times. Chemicals spilled on the ground must be washed and broken glassware
must be swept off immediately. Mops, brooms, dust-pans etc will be available
from the preparation room.
Some important information regarding

the 33rd IChO practical examination
Time duration for the practical examination would be four
and a half hours instead of five hours.
The examination may consist of three independent

experimental tasks. The time duration for each task may
vary from one to one and a half hour.
The examination will be conducted in two batches.

Students No.1 and 2 from each team will be part of the
first batch; students No.3 and 4 will be part of the second
batch.
Students of both batches will get a new set of apparatus

for the examination.
The apparatus for the examination will include both

plasticware and glassware.
The examination will not involve use of microscale

apparatus.

Problem 25 Determination of aspirin in the given sample
Acetyl salicylic acid (CH3COO.C6H4.COOH) undergoes hydrolysis when boiled gently

with aqueous NaOH, which forms a basis for its estimation.
Chemicals and solutions
• Plain aspirin tablets
• 0.1 M Hydrochloric acid R : 34, 37 S : 26, 45
• 1 M Sodium hydroxide R : 35 S : 2, 26, 37, 39
• Borax(AR Grade) S : 22, 24, 25
• Phenol red indicator S : 22, 24, 25
Preparation of 0.1 M HCl solution
9 mL of concentrated HCl is diluted to 1000 mL using freshly prepared distilled water in

a standard volumetric flask.
Preparation of 1 M NaOH solution.
Weigh rapidly approximately 10.5 g of NaOH in a small beaker. Dissolve it in minimum

amount of distilled water. Transfer the solution in a 250 mL flask and dilute the solution
using boiled out distilled water.
Procedure
Standardisation of HCl
Weigh 0.15 g of Borax accurately and transfer it quantitatively in a clean 250 mL

conical flask ; add 50 mL of distilled water to the flask. Titrate the resulting solution with
HCl, using methyl red indicator until the colour changes from yellow to red.
Calculate the concentration of the HCl solution.

Blank titration
Dilute the 25 mL of 1 M NaOH solution in a 250 mL standard flask using freshly boiled
distilled water. Pipette out 25 mL of the diluted NaOH solution and titrate it against the
HCl solution using phenol red as indicator until the colour changes from red to yellow.
Titration of sample aliquot
Weigh accurately about 1.5 g of the crushed tablet sample and transfer it
quantitatively in a 250 mL beaker. Add 25 mL of 1 M NaOH solution with the help of
pipette and swirl the content. Boil the mixture gently on a water bath for 15 min and
then cool the solution. Transfer the solution to a 250 mL standard flask. Dilute the
solution up to the mark with distilled water and mix well. Titrate 25 mL of the diluted
solution against the standardised HCl solution using phenol red indicator until the
colour changes from red to yellow.
Write down the appropriate chemical reaction for hydrolysis of acetyl

salicylic acid.
Calculate the percentage of aspirin in the sample.
Problem 26 Synthesis of 1-phenyl-azo-2-naphthol (C16H12ON2)
Reactions
+ - + -
NH3Cl N NCl
NH2
HCl Diazotization
(NaNO2 + HCl)
Aniline Salt Benzene Diazonium

Chloride Salt
+ -
N NCl N N
OH OH
+ NaOH
Coupling
Benzene Diazonium Sudan - 1
Chloride Salt lB-napthol
(1-phenyl-azo-2-napthol)

• Aniline R : 23, 24, 25, 33 S : 28, 36, 37, 45
• Concentrated HCl R : 34, 37 S : 26, 45
• Solid Sodium Nitrite R : 8, 25 S : 44
• β - naphthol R : 20, 22 S : 24, 25
• Ethyl Alcohol
• Urea S : 22, 24, 25
• Sodium Hydroxide R : 35 S : 2, 26, 37, 39
Preparation of diazonium salt
Take 1 mL of aniline in a clean 50 mL beaker. Add approximately 5 mL of distilled

water to aniline. Place the beaker in an ice-bath. Slowly add 2.5 mL of conc. HCl.
Stir the solution with a glass rod to obtain a clear solution. Cool this solution in the
ice-bath.
Weigh accurately 0.5 g of sodium nitrite (NaNO2) and transfer it quantitatively in a 15

(or 25) mL test tube. Add 5mL of distilled water (to the test tube) to dissolve NaNO2.
Cool the resulting NaNO2 solution in an ice-bath.
Allow both the solutions to attain 0°C temperature. Add sodium nitrite solution in a
dropwise manner to the aniline solution with continuous stirring. (During addition, the
temperature of the reaction mixture should not rise above 10°C.)
The presence of excess nitrous acid in the reaction mixture is checked using starch
iodide paper.
To decompose the excess nitrous acid formed, add a small portion of solid urea. The
solution is then filtered. The filtrate contains the diazonium salt.

Coupling reaction
Weigh 0.75 g of powdered β-naphthol in a 50 mL beaker. Add 5 mL of 10% NaOH

solution and 5 mL of distilled water to the beaker. Stir well with glass rod to obtain a
clear solution. This solution is also cooled in an ice-bath to 0°C.
The ice cooled filtrate containing diazotised salt is added dropwise to the ice cooled
solution of β-naphthol with constant stirring. At this stage, an orange-red dye will
start precipitating. After the addition of the solution is complete, filter the dye using
buchner funnel. Cold water is used for washing the precipitate. Dry the product and
record the yield.
Determination of melting point
Recrystallise a small portion of the organic dye prepared using ethyl alcohol. Gently
heat the solution in a water bath (careful!) to dissolve the dye. Filter the hot solution.
Cool the filtrate and filter the recrystallised product using Buchner funnel and suction.
Record the weight of the crude product
Record the melting point of the recrystallised product.
Problem 27 Determination of calcium in a sample solution
Reaction
2+ 2- 2- +
Ca + H2Y CaY + 2H
Chemical and solutions
• Sample solution containing calcium R : 36 S : 22, 24

(prepared from A.R. grade CaCl2)
• Patton and Reeders indicator

• KOH solution. R : 35 S : 26, 37, 39, 45
• EDTA disodium salt R : 36, 37, 38 S : 26, 36
Preparation of 0.01 M EDTA:
Weigh 1.861 g of AR grade Na2EDTA and quantitatively transfer the same to 500
mL volumetric flask. Add distilled water to the flask to dissolve Na2EDTA and make
up the solution to 500 mL mark with distilled water.
Procedure
Dilute the given sample solution to 100 mL in a 100 mL volumetric flask using
distilled water. Pipette out 25 mL of the diluted sample solution in a clean conical
flask. Add 25 mL of distilled water and adjust the pH using freshly prepared KOH
solution to 12. Check the pH with pH paper. Add a pinch of solid indicator and titrate
with Na2EDTA solution till the colour changes from wine red to blue.
Calculate the amount of calcium in mmoles in 100 mL of the diluted

sample solution
Problem 28 Estimation of methyl ketone by back titration
Methyl ketones like acetone can be estimated by iodinating with excess of standard
iodine in an alkaline medium. The unreacted iodine is then back titrated with
standard sodium thiosulphate solution.
• 0.1N Iodine solution R : 20, 21 S : 23, 25
• 0.1N NaOH R : 35 S : 2, 26, 37, 39
• Concentrated HCl R : 34, 37 S : 26, 45
• 1 N H2SO4. R : 35 S : 2, 26, 30
• 0.1 M Na2S2O3 S : 22, 24, 25

Preparation of 0.1 M Na2S2O3:
Weigh 25 g of AR grade Na2S2O3 and quantitatively transfer it to a 1 L volumetric

flask. Prepare the solution using freshly boiled distilled water. Add 3 drops of
chloroform while preparing the solution. Avoid exposure to light.
Preparation of 0.1 N I2 solution
Dissolve 20 g of iodate-free potassium iodide in 30 - 40 mL of distilled water in a 1 L

volumetric flask. Weigh 12.7 g iodine and quantitatively transfer to the concentrated
potassium iodide solution. Shake the flask well until all the iodine dissolves and then
dilute up to the mark with distilled water.
Procedure
Standardisation of Na2S2O3
Weigh out accurately 0.14 to 0.15 g of dry potassium iodate. Dissolve it in 25 mL of

distilled and freshly boiled water and add 2 g of iodate free potassium iodide. Add 5
mL of 1N sulphuric acid. Titrate the liberated iodine with thiosulphate solution with
constant shaking. When the colour of the solution is pale yellow add 200 mL of
distilled water and 2 mL of starch indicator. Continue the titration until the colour
changes from blue to colourless.
Determination of ketone
Weigh accurately 0.2 g of the given acetone sample in a clean 50 mL beaker and
add minimum amount of distilled water. Transfer the acetone solution to a 250 mL
standard volumetric flask. Add distilled water to the flask to prepare acetone solution
in water and make up the solution to 250 mL mark with distilled water. Pipette out 10
mL of the acetone solution in a clean conical flask. Add 10 mL of 10% aqueous
sodium hydroxide, and stopper the flask. Shake the flask for 10 min. At the end of 10
minutes, add 35 mL of 0.1 N Iodine solution from the burette. Swirl the content,
preferably using magnetic stirrer for 5 minutes, and keep it standing for 15 minutes.
Yellow crystals of iodoform will appear. Acidify the solution with H2SO4 (check the pH
with pH paper).

Titrate the solution against the standardised sodium thiosulphate using starch
indicator.
Write down the appropriate chemical reactions for iodination of

acetone.
Calculate the amount of acetone in the given sample solution.
Problem 29 Determination of phenol in the given sample.
Reactions
KBrO3 + 5KBr + 6HCl → 6KCl + 3H2O + 3Br2 ↑
C6H5OH + 3Br2 → C6H2OHBr3 + 3HBr
3Br2 + 6KI → 6KBr + 3I2 ↑
6Na2S2O3 + 3I2 → 3Na2S2O3 + 6NaI
• 0.3g phenol R : 24, 25, 34 S : 2, 28, 44
• 0.02M KBrO3 R:9 S : 24, 25, 27
• 3M H2SO4 R : 35 S : 2, 26, 30
• KBr
• KI S : 22, 24, 25
• 1 M Na2S2O3 S : 24, 25, 28
• Starch indicator.

Preparation of 0.1 M Na2S2O3
Weigh 25 g of AR grade Na2S2O3 in a small beaker. Quantitatively transfer it to a 1 L

volumetric flask. Prepare the solution using freshly boiled distilled water. Add 3 drops
of chloroform while preparing the solution. Avoid exposure to light.
Standardisation of Na2S2O3
Weigh out accurately 0.14 to 0.15 g of dry potassium iodate. Dissolve it in 25 mL of

fresh, boiled distilled water and add 2 g of iodate free potassium iodide. Add 5 mL of
1N sulphuric acid. Titrate the liberated iodine with thiosulphate solution with constant
shaking. When the colour of the solution is pale yellow add 200 mL of distilled water
and 2 mL of starch indicator. Continue the titration until the colour changes from blue
to colourless.
Procedure
Dissolve the given sample of phenol to 250 mL with distilled water. Take 25 mL of
the phenol solution into 250 mL stoppered conical flask. Add 25 mL of standard
potassium bromate solution and 0.5 g of potassium bromide. Add 5 mL of 3M
sulphuric acid. Stopper the flask immediately. Mix the reagents and let them stand
for 15 min (avoid exposure to light). Then, add 2.5 g of potassium iodide rapidly. Re-
stopper the flask immediately and swirl the contents of the flask to dissolve the solid.
Titrate the liberated iodine with standard 0.1M Na2S2O3 from the burette using starch
indicator.
Calculate the amount of phenol per 250 mL of the solution.
Problem 30 Determination of amount of Fe (III) present in the given

sample
Fe (III) in the sample solution is first reduced to Fe (II) in HCl medium using stannous
chloride. Excess of stannous chloride is oxidized by addition of mercury (II) chloride.
The Fe(II) is then titrated with standard potassium dichromate solution.

• Sample solution R : 36, 38 S : 26, 36

• 0.1N K2Cr2O7 solution R : 45, 36, 37, 38, 43 S : 53, 22, 28
• Equimolar H2SO4 & R : 35 S : 2, 26, 30
H3PO4 acid mixture R : 34 S : 26, 45
• Conc. HCl R : 34, 37 S : 26, 45
• 5% HgCl2 R : 26, 27, 28 S : 13, 28, 45
• 3% SnCl2 solutions R: 22, 36, 37, 38 S : 26, 36,
• Diphenylamine indicator. R : 23, 24, 25, 33 S : 28, 36, 37, 45
Note : NH4Fe(SO4)2.12H2O is used to prepare the sample solution
Preparation of 0.1N K2Cr2O7 solution
Weigh accurately 1.225 g of pure K2Cr2O7 and transfer it to a 250 mL volumetric

flask. Prepare the solution using distilled water.
Procedure:
Dilute the given Fe(III) sample solution to 100 mL using the standard volumetric
flask. Take 10 mL of the diluted sample solution in a clean conical flask. Add 2 mL of
concentrated HCl and boil the solution. To the hot solution, add SnCl2 solution
dropwise till the reaction mixture becomes colourless. Add 2 - 3 drops of SnCl2 in
excess.
Cool the solution under tap water. Add 2 to 3 mL of HgCl2 solution at once. A white
precipitate is obtained at this stage. (If grey precipitate is obtained, reject the sample
and start again.)
Add 2 to 3 mL of the acid mixture and 1 drop of the diphenylamine indicator and
titrate it against K2Cr2O7 solution. Continue the titration until a colour change from
colourless to permanent blue or violet is observed.
Write down the appropriate chemical reactions .
Calculate the amounts of Fe (III) and NH4Fe (SO4) 2 12H2O per 100 mL
of the sample solution.

Worked Solutions to Problems
1. Water
A. Phase diagram
a. The three phases of water coexist in equilibrium at a unique temperature and

pressure (called the triple point):
Ttr = 273.16 K = 0.01 °C Ptr = 6.11 x 10−3 bar
b. If pressure decreases, boiling point decreases, but melting point increases

(slightly).
c. Beyond this point, there is no distinction between liquid and vapour phases of
water. Put alternatively, it is possible to have liquid to vapour transition by a
continuous path going around the critical point. (In contrast, solid-liquid
transition is discontinuous.)
d. T = 300K, P = 12.0 bar : liquid phase

T = 270K, P = 1.00 bar : solid phase
e. Below P = 6.11 x 10−3 bar, ice heated isobarically will sublimate to vapour.
f. If xl and xv are the mole fractions of water in liquid and vapour phases,
V = xl V l + x v V v = x l Vl + (1 − x l ) V v
Vv − V
∴ xl = = 4.6 x 10 −1
V v − Vl
Vl x l Vl
= = 0.140
V V
Vv
= 1 − 0.14 = 0.860
V

B. Clausius – Clapeyron equation
a. dP ∆H
=
dT T ∆V
∆H = molar enthalpy change in phase transition
∆V = molar change in volume in phase transition.
For ice-liquid water transition :
∆H > 0 ∆V < 0, since ice is less dense than water.

dP
∴ < 0
dT
Since ∆ V is not large, the P-T curve for this transition is steep, with a
negative slope. Thus decrease of pressure increases the melting point
slightly.
For liquid water - vapour transition
∆H > 0 ∆< 0
dP
∴ > 0
dT
Decrease of pressure decreases the boiling point.
b. Clausius - Clapeyron equation for (solid) liquid - vapour transition is
dP P ∆Hvap
=
dT RT 2
This equation follows from the Clapeyron equation under the assumptions:
1. Vapour follows ideal gas law.
2. Molar volume of the condensed phase is negligible compared to molar

volume of vapour phase.
3. If further ∆Hvap is assumed to be constant (no variation with T), the eq.
is integrated to give
P2 ∆Hvap 1 1
ln =  − 
P1 R T
 1 T2 

Here P1 = 1.01 bar , T1 = 373.15 K

−1
T2 = 393.15 K ∆Hvap = 40.66 kJ mol
R = 8.31 J K−1 mol-1
∴ P2 = 2.01 bar
The estimate is based on assumptions 1, 2 and 3.
c. For ice - liquid water equilibrium, use Clapeyron equation
At T1 = 273.15 K, P1 = 1.01 bar
∆H
1. Assume that for a small change in T, is constant.
∆V
Integrating the Clapeyron equation above
∆H T 
P2 − P1 = ln  2 
∆V  T1 
T2 = 272.95 K, ∆H(fusion) = 6008 Jmol−1
 1 1  −6 −1
∆V =  −  x 18.015 = − 1.63 x 10 m mol
3
 1.00 0.917 
P2 − P1 = 27 bar
P2 = 28 bar
The estimate is based on assumption 1.
C. Irreversible condensation
a. On the P-T plane, this equilibrium state is a solid phase (ice). Water in liquid
phase at this temperature and pressure is not an equilibrium state - it is a
supercooled state that does not lie on the given P-T plane.
b. Treating the metastable state as equilibrium state, we can go from the

supercooled liquid state to the solid state at the same temperature and
pressure by a sequence of 3 reversible steps.
1. Supercooled liquid at -12.0°C to liquid at 0°C
q1 = number of moles x Cp (liquid water) x change of temperature

28.5g
−1
x 76.1 J K −1 mol−1 x 12.0 K = 1445 J
18.015 g mol
2. liquid at 0°C to ice at 0°C
q2 = 28.5 g x (−333.5) J g−1 = − 9505 J
3. Ice at 0°C to ice at −12.0°C
q3 = number of moles x Cp (liquid water) x change of temp.
28.5
= −1
x 37.15 J K −1 mol−1 x (− 12.0 K )
18.015 g mol
= − 705.3 J
∴ q = q1 + q2 + q3 = − 8765 J
Since all the steps are at the constant pressure of 1.00 bar,
q = ∆H
But ∆H is independent of the path, i.e., it depends only on the end points.
Thus for the irreversible condensation of supercooled liquid to ice
q = ∆H = −8765 J
c. The actual irreversible path between the two end states of the system is
replaced by the sequence of three reversible steps, as above. For each
reversible step, ∆S can be calculated.
T2
Cp T2
∆S1 = n ∫
T1 T
dT = n Cp ln
T1
28.5 g 273.15
∆S1 = −1
76.1 J K −1 mol−1 x ln
18.015 g mol 261.15
= 5.41 J K−1

∆H2 − 9505
∆S 2 = = = − 34.79 J K −1
T 273.15
28.5 g 261.15
∆S3 = −1
37.15 J K −1 mol −1 ln
18.015 g mol 273.15
= − 2.64 J K−1
∆Ssystem = ∆S1 + ∆S2 + ∆S3 = − 32.02 J K −1
qsur 8765
∆Ssur = = = 33.56 J K −1
Tsur 261.15
∆Suniv = ∆Ssystem + ∆Ssur = 1.54 J K −1
The entropy of the universe increases in the irreversible process, as expected

by the Second Law of Thermodynamics.
2. van der Waals gases
a. For a van der Waals gas

PV bP na n2 a b
Ζ = = 1+ − + 2
nR T RT VRT V RT
The ratio of the magnitudes of the second and third terms on the right side is :
b b
PV ≈ RT, taking PV = nRT up to zeroth order.
na a
The ratio of the magnitudes of the fourth and third terms on the right side is :
nb bP
≈
V RT
i. From the ratios above, it follows that at sufficiently high temperature for
any given pressure, the second term dominates the third and fourth
terms. Therefore,
bP
Ζ ≅ 1+ > 1
RT
For small P, Z nearly equals unity.

ii. At lower temperatures, the third term can be greater (in magnitude)
than the second term. It may be greater (in magnitude) than the fourth
term also, provided P is not too large. Since the third term has a
negative sign, this implies that Z can be less than unity.
iii. For a = 0
bP
Ζ = 1+
RT
which shows that Z increases linearly with P.
b. Helium has negligible value of a. Graph (1) corresponds to He and (2)

corresponds to N2.
c. Above T > Tc, only one phase (the gaseous phase) exists, that is the cubic
equation in V has only one real root. Thus isotherm (2) corresponds to T < Tc .
d. At T = Tc , the three roots coincide at V = Vc This is an inflexion point.
dP d2P
= = 0
dV V dV 2 V
c c
The first condition gives

RTc 2na
= (1)
(Vc − nb) 2
Vc
3
The second condition gives

RTc 3na
= (2)
(Vc − n b) 3
Vc
4
These equations give

8a
Vc = 3 n b and Tc =
27b R
For He, Tc = 5.2 K
For N2, TC = 128K
Since, Tc (N2) is greater than Tc (He), N2 is liquefied more readily than He.

V2
e.
W = ∫ P dV
V1
V2
 RT a 
= ∫ − 2  dV
V
 V −b V 
1
 V −b  1 1
= RT ln  2  + a  − 
 V1 − b   V2 V1 
= 56.7 L bar mol− 1
3. Rates and reaction mechanisms
a. Mechanism 1 :
1 d [H I]
= k1 [I]2 [H2 ]
2 dt
Since the first step is fast, there is a pre - equilibrium :
[I]2
K =
[I2 ]
d[HI]
∴ = 2 k1 K [I2 ] [H2 ] = k [H2 ] [I2 ]
dt
Mechanism 2 :
1 d [HI]
= k 2 [I2 ]d [H2 ]
2 dt
[I ]
K' = 2 d
[I2 ]
d [HI]
∴ = 2 k 2 K' [I2 ] [H2 ] = k [H2 ] [I2 ]
dt
Both mechanisms are consistent with the observed rate law.

− Ea
b. i. k = Ae RT
1 1 k
Ea  −  = R ln 2
 T1 T2  k1
With the given numerical values,
Ea = 170 kJ mol− 1

ii. The activation energy is greater than the bond dissociation energy of
I2. Hence the second step is rate determining in both the mechanisms.
c. The activation energy Ea’ for the reverse reaction is
E'a = Ea − ∆U
= 170 + 8.2 = 178.2 kJ mol− 1
d. i.
d [I2 ]
= k 3 [IAr] [I]
dt
[IAr][Ar]
K' ' =
[I][Ar]2
d [I2 ]
∴ = K ' ' k 3 [I]2 [Ar]
dt
= k [I]2 [Ar]
ii. A possible reason why this is negative is that Ea3 is positive and less in
magnitude than ∆H°, while ∆Ho is negative.
k = k 3K ' '
°
−
E a3
− ∆G
= A 3e RT
e RT
we know ∆ G° = ∆ Η° − T∆ S °
∆S° (Ea3 + ∆ Η° )
−
∴ k = A3 e R
e RT
The activation energy for the overall reaction is E a3 + ∆ Η°
4. Enzyme catalysis
a. i. The differential rate equations for the Michaelis-Menten mechanism are
d [ES]
= k1 [E] [S] - k1' [ES] − k 2 [ES] (1)
dt
d[P]
= k 2 [ES] (2)
dt

d[ES]
In the steady-state approximation, = 0 (3)
dt
Eq. (1) then gives [ES] = k1 [E] [S] (4)
k1' + k 2
Now [E] 0 = [E] + [ES] (5)
where [E]0 is the total enzyme concentration. Eqs. (4) and (5) gives
[E]0 [S]
[ES] = (6)
K m + [S]
k 1' +k 2
where K = is the Michaelis-Menten constant.
m k1
d[P] k 2 [E]0 [S]

From eq. (2), = (7)
dt K m + [S]
Since the backward rate is ignored, our analysis applies to the initial rate of
formation of P and not close to equilibrium. Further, since the enzyme
concentration is generally much smaller than the substrate concentration, [S]
is nearly equal to [S]0 in the initial stage of the reaction.
Thus, according to the Michaelis-Menten mechanism, the initial rate versus

substrate concentration is described by eq. (7), where [S] is replaced by [S]0.
For [S] << Km,
k2
Initial rate = [E]o [S] (8)
Km
i.e., initial rate varies linearly with [S].
For [S] >> Km,
Initial rate = k2 [E]0 (9)
i.e., for large substrate concentration, initial rate approaches a constant

value k2 [E]0.
Thus the indicated features of the graph are consistent with Michaelis-Menten
mechanism.

ii. The asymptotic value of initial rate is k2 [E]0
From the graph,
k2 [E]0 = 3.0 x 10-6 M s−1
With [E]0 = 1.5 x 10−9 M
we get k2 = 2.0 x 103 s−1
iii. From eq. (7), for [S] = Km, the initial rate is half the asymptotic value.
From the graph, therefore,
Km = 5.0 x 10−5 M
For [S] = 1.0 x 10−4 M, using eq. (7) again,
[2.0 x 103 s−1] x [1.5 x 10 −9 M] x [1.0 x 10 −4 ]M

Initial rate =
[5.0 x 10 − 5 ] M + [1.0 x 10 − 4 ] M
= 2.0 x 10 −6 M s −1
k1| +k 2
iv. We have Km = = 5.0 x 10−5 M
k1
The enzyme equilibrates with the substrate quickly, that is the first step
|
of equilibration between E, S and [ES] is very fast. This means that k1
is much greater than k2. Therefore, neglecting k2 above,
k1|
= 5.0 x 10 − 5 M
k1
The equilibrium constant K for the formation of ES from E and S is,
K k
= 1| = 2.0 x 10 − 5
1M k1
b. From the graph at the new temperature, k2 [E]0 = 6.0 x 10−6 M s−1
6.0 x 10 −6 M s−1
i.e., k2 = −9
= 4.0 x 103 s −1
1.5 x 10 M

Using Arrhenius relation for temperature dependence of rate constant :

E
− a
k = A e RT
(10)
where Ea is the molar activation energy.

Ea  1 1 
−  − 
k(T1 ) R  T1 T2 
= e
k(T2 )
k(T2 )
ln
k(T1 )
i.e. Ea = R (11)
1 1
 − 
 T1 T2 
k 2 (310)
Now = 2.0 , R = 8.31 J K−1 mol−1
k1(285)
∴ Ea = 20.4 kJ mol−1
c. i. The fraction of the enzyme that binds with the substrate is, from eq.
(6):
[ES] [S] (12)
=
[E]0 K m + [S]
where [S] is nearly equal to [S]0 in the initial stage of the reaction.
3.0 x 10 −6 mol
Now [S]0 = = 3.0 x 10 − 3 M
1 x 10 −3 L
and Km = 5.0 x 10−5 M
[ES] 3.0 x 10 −3 M
∴ = = 0.98
[E]0 (5.0 x 10 − 5 + 3.0 x 10 − 3 )M
Nearly the whole of the enzyme is bound with the substrate.
ii. From eq. (7),

Integrating the equation gives,
d[S] k 2 [E]0 [S]
= −
dt K m + [S]

[S] (13)
K m ln + [S] − [S]0 = − k 2 [E]0 t
[S]0
If at t = T, [S] = 1/2[S]0,
1
T k 2 [E]0 = K m ln 2 + [S]0 (14)
2
2.0 x 10 −12 mol
Here [E]0 = = 2.0 x 10 − 9 M
1.0 x 10 − 3 L
k2 = 2.0 x 103 s−1, Km = 5.0 x 10−5 M,
[S]0 = 3.0 x 10−3 M
Substituting these values in eq. (14) gives
T = 384 s
Thus 50% of the antibiotic dose is inactivated in 384 s.
d. i. The differential rate equations for the situation are :
d
[ES] = k1 [E] [S] − k|1 [ES] − k 2 [ES] (15)
dt
d
[EI] = k 3 [E] [I] − k |3 [EI] (16)
dt
d
[P] = k 2 [ES] (17)
dt
|
where k3 and k 3 are the forward and backward rate constants for the
enzyme-inhibitor reaction.
Applying steady-state approximation to [ES] and [EI],

k1 [E] [S] (18)
[ES] =
k1| + k 2
k 3 [E] [I]
and [EI] = (19)
k |3
Now [E]0 = [E] + [ES] + [EI] (20)

Eliminating [E] and [EI] from eqs. (18) to (20) gives :

[E]0 [S]
[ES] = (21)
 [I] 
[S] + K m 1 + 
 K I (1M) 
d[P] k 2 [E]0 [S]

= (22)
dt  [I] 
[S] + K m 1 + 
 K I (1M) 
k |3
Here, K I (1M) = is the equilibrium constant for the dissociation of EI
k3
to E and I.
r
The degree of inhibition is i = 1−
r0
Km [I]
KI (1M)
Using eq. (22), i = (23)
 [I] 
[S] + K m 1 + 
 K I (1M) 
For fixed [I], i decreases with increase in [S] (competitive inhibition).
and for large [S], i → 0, i.e., the inhibitor ceases to play any role.
[I]
ii. For small [S] i =
K I (1M) + [I]
1 3
If r = r0, i =
4 4
i.e., [I] = 3 KI x (1M) = 1.5 x 10−4 M
The inhibitor concentration required to reduce the rate of inactivation by

a factor of 4 is 1.5 x 10−4 M; i.e., 0.15 µmol in a volume of 1.00 mL.

5. Schrödinger equation
a.
i. One-dimensional Schrödinger equation for a free particle of mass m:
h2 d2ψ h
− = Eψ h=
2m dx 2 2π
where E stands for the energy of the particle and ψ its wave function.
ii. The boundary conditions are :
ψ (0) = ψ(L) = 0
nπ x
Only ψn (x) = sin satisfies the required boundary conditions.
L
Other functions are not possible wave functions of the electron in a

one-dimensional rigid box.
iii.
h 2 d2 nπ x h 2π 2 2 nπ x
− sin = n sin
2m dx 2 L 2 L
2mL
h 2π 2 h2n2
∴ En = n2 =
2mL2 8mL2
iv. Ground state (n = 1)

ψ1(x)
πx
ψ1 (x) = sin 0 L
L x
First excited state (n = 2) ψ2(x)
0 L
2πx x
ψ2 (x) = sin L/2
L ψ3(x) x
Second excited state (n = 3) 0 L
L L/3 2L/3
3πx
ψ3 (x) = sin
L
Number of nodes in ψn = n −1, apart from the nodes at the end
points.

v.
πx
ψ 1N (x) = N sin
L
∞ 2
1 = ∫ ψ 1N (x) dx
−∞
L L
2 2 πx N2  2πx
=N ∫ sin L
dx =
2 ∫  1 − cos  dx
L 
0 0
L
= N2
2
2
∴ N = ( N is chosen to be real )
L
2 πx
ψ 1N (x) = sin
L L
b. In the example
L = 5 × 1.4 × 10−10 m = 7.0 × 10−10 m
The first three energy levels are:
h2
E1 = = 1.22 × 10 −19 J
8mL2
E2 = 4 E1 = 4.88 × 10 −19 J
E3 = 9 E1 = 10.98 × 10 −19 J
In the ground state, the four electrons will occupy the levels E1 and E2, each
with two electrons.
E3 E3
E2 E2
E1 E1
Ground state Lowest excited state

The lowest excitation energy
E3 – E2 = 6.10 × 10 –19 J
c. The condition that ψ(φ) is single valued demands that
ψ (φ) = ψ (φ + 2π)
eiλφ = eiλ(φ+2π)
ei 2πλ =1
i.e. λ =m, where m = 0, ±1, ±2, ±3,…….
This shows that angular momentum projection (Lz) cannot be an arbitrary real
number but can have only discrete values: mh, where m is a positive or
negative integer (including zero).
6. Atomic and molecular orbitals
A. Atomic orbitals
a. r
−
i. N
ψ 1s = Ne ao
2
= ∫ dv = 4 π a 3o N 2
N
1 ψ 1s
a 3o
=4πN x = π a 3o N 2
2
(N chosen to be real)
4
[πa ]
1
3 −2
∴ N = o
r
[π ] −
1 −
N
ψ 1s = a 3o 2 e ao
ii. Probability of finding an electron between r and r + dr

2r
[ ] −1 −
= 4π r 2
x πa30 e a0
dr
This is a maximum at r = rmax , given by
 −
2r 
d  r 2 e a0  = 0
dr  
  r =rmax
This gives
rmax = a0
The 1s electron is most likely to be found in the neighborhood of r = a0.
b. ψ 2s =0 at r = 2a0
Nodal surface is a sphere of radius 2a0

π
ψ2p z = 0 at θ =
2
Nodal surface is the xy plane.

 1 
ψ3d = 0 at 3cos2θ − 1 = 0, i.e., θ = cos −1  ± 
z2  3
Nodal surfaces are cones with these values of half-angle, one above the xy
plane and the other below it.
(Note: all three wave functions vanish as r → ∞. At r = 0, ψls does not vanish,
but the other two wave functions vanish.)
c. Each electron in n = 1 shell of helium atom has energy − Z2eff × 13.6 eV
Helium ground state energy = − Z2eff × 27.2 eV
Energy of He+ ground state = − 4 × 13.6 = − 54.4 eV
Ionization energy = (− 54.4 + Z2eff × 27.2) eV = 24.46 eV
This gives Zeff = 1.70
B. Molecular orbitals
a. ψ1 and ψ 2 are bonding orbitals

~ and ψ
ψ ~ are antibonding orbitals
1 2
Bonding orbital
No nodal surface between the nuclei. Electronic energy has a minimum at a
certain internuclear distance. Qualitative reason: electron has considerable
probability of being between the nuclei and thus has attractive potential
energy due to both the nuclei.

Antibonding orbital
Nodal surface between the nuclei. Electronic energy decreases monotonically
with internuclear distance. Hence bound state is not possible.
b. Re = 1.32 × 10−10 m
D = −1.36 – (−15.36) = 1.76 eV
c. It will dissociate to a hydrogen atom in 2s state and a bare hydrogen nucleus

(proton).
d. The two electrons occupy the same molecular orbital with the lowest energy.
By Pauli’s principle, their spins must be antiparallel. Hence the total electronic
spin is zero.
e. In the first excited state of H2, one electron is in ψ1 (bonding orbital) and the
other in ψ1 (antibonding orbital). It will dissociate into two hydrogen atoms.
f. Using the aufbau principle, in the ground state two electrons of He2 are in ψ1
(bonding orbital) and two in ψ1 (antibonding orbital). The bond order is
½ (2 −2) = 0
Therefore, bound He2 is unstable and difficult to detect. However, if one or
more electrons are elevated from the antibonding orbital to (higher energy)
bonding orbitals, the bond order becomes greater than zero. This is why it is
possible to observe He2 in excited states.
7. Fission
a.
235
92 U + n → 94
38 Sr + 140
54 Xe + 2n
235
92 U + n → 141
56 Ba + 92
36 Kr + 3n
b. The net nuclear reaction is

235
92 U + n → 94
40 Zr + 140
58 Ce + 2n + 6e − + (Q)
The energy released is
Q = [m N ( 235 U) − m N ( 94 Zr) − m N ( 140 Ce) − m n − 6m e ] c 2

where the small energy of the initial thermal neutron has been ignored. (mN
denotes the nuclear mass.) Now
m N(
235
U) = m ( 235 U) − 92m e
ignoring the small electronic binding energies compared to rest mass energies.
Similarly for other nuclear masses.
Q = [m ( 235 U) − m (94 Zr) − m (140 Ce) − m n ] c 2
Using the given data,
Q = 213.3 MeV
c. 1 MWd = 106 Js−1 x 24 x 3600 s = 8.64 x 1010 J
8.64 x 1010
No. of atoms of 235 U fissioned = = 2.53 x 10 21
213.3 x 1.60 x 10 − 13
235 2.53 x 10 21 x 235

Mass of U fissioned = = 0.99 g
6.02 x 10 23
Mass of 235U in 1 kg uranium removed from the reactor = 7.2 − 0.99 = 6.2 g
235
Abundance of U is 0.62 %
8. Radioactive decay
a. 1µCi = 3.7 x 104 disintegrations per second (dps).
Initial β −activity = 3.7 x 106 dps
− dN1
= N1o λ1 = 3.7 × 10 6 dps
dt t = 0
where N1o is the number of atoms of 210
Bi at t = 0 and λ1 is its decay
constant .

0.693
N10 = 3.7 × 10 6
5.01 × 24 × 3600
N10 = 2.31 × 10 12
210
Intial mass of 210
Bi = 2.31 × 10 12 × g
6.02 × 10 23
= 8.06 × 10 −10 g
b. Number of atoms of 210Bi at time t is given by
N1 = N10 e − λ1t
The number of atoms of 210Po, N2, is given by equation
dN 2
= λ 1N 1 − λ 2 N 2
dt
210
where λ 2 is the decay constant of Po.
dN2
= λ1 N10 e- λ1t − λ 2 N2
dt
λ2t
Using the integrating factor e
dN2
eλ2t + λ 2 N2 e λ 2 t = λ1 N10 e(λ 2 − λ1 )t
dt
d λ 2t
(N2 e ) = λ1 N10 e(λ 2 − λ1)t
dt
Integrating
λ1
N2 e λ 2 t = N10 e(λ 2 − λ1)t + C
λ 2 − λ1
To calculate C, use the condition that at t = 0, N2 = 0

λ 1 N 10
C = −
λ 2 − λ1
This gives
λ1
N2 = N10 (e− λ1t − e− λ 2 t )
λ2 − λ1

The time t = T when N2 is maximum is given by the condition
dN2
=0
dt t =T
which gives
λ1
ln
λ2
T= = 24.9 d
λ1 − λ 2
At t = T, N2 can be calculated from above.
N2 = 2.04 x 1012
Mass of 210Po at t = T,
= 7.11 x 10−10 g
c. α-disintegration rate of 210Po at t = T
= 1.18 x 105 dps
At t = T
β - disintegration rate of 210Bi
= α-disintegration rate of 210

Po = 1.18 x 105 dps
9. Redox reactions
a.
i. Over-all reaction
Sn 2 + + 2Fe 3 + → Sn 4 + + 2Fe 2 + E° = + 0.617 V
∆ G ° = − nFE ° = − 2FE °
= − 2 × 96485 × 0.617 V
= − 119 KJ

ii.
E° =
0.0592
logK
n
(2 × 0.617)
log K = ≅ 20.84
0.0592
20
K = 6.92 × 10
b. Before the equivalence point, E of the cell is given by following equation

2+
0.0592 [Sn ]
E cell = ox E o
+ red E o
− log 4+
S.C.E Sn 4 + /Sn 2 + 2 [Sn ]
2+ ]
0.0592 [Sn
= − 0.242 + 0.154 − log 4+
2 [Sn ]
i. The addition of 5.00 mL of Fe3+ converts 5.00/20.00 of the Sn2+ to

Sn4+; thus
2+
[Sn ] 15.0/20.0
4+
= = 3.00
[Sn ] 5.0/20.0
Ecell = − 0.102 V.
ii. At the equivalence point, add the two expressions corresponding to

Sn4+/Sn2+ and Fe3+/Fe2+ .
2+
= 2 ox E°S.C.E + 2 E°
[Sn ]
2 Ecell − 0.0592 log 4+
Sn 4 + /Sn 2 +
red
[Sn ]
2+
= ox E°S.C.E + E°
[Fe ]
1 Ecell − 0.0592 log 3+
Fe 3 + /Fe 2 +
red
[Fe ]
to get
2+
2+
= 3 ox E° + 2 redE° + red E°
[Sn ][Fe ]
3 E − 0.0592 log 4+ 3+
cell S.C.E Sn 4 + /Sn 2 + Fe 3 + /Fe 2 + [Sn ][Fe ]

At the equivalence point, [Fe3+] = 2 [Sn2+] and [Fe2+] = 2 [Sn4+]

Thus,
2 Eo + Eo
red Sn 4 + /Sn 2 + Fe 2 + / Fe 3 +
red
E cell = ox EoS.C . E +
3
(2)(0.154) + 0.771
= − 0.242 + = + 0.118 V
3
Beyond the equivalence point, E of the cell is given by following equation

2+
[Fe ]
E cell = E o
+ E o
− 0.0592 log
ox S.C.E red Fe3 + /Fe 2 + 3+
[Fe ]
When 30 mL of Fe3+ is added , 10 mL of Fe3+ is in excess. i.e.

2+
[Fe ] 20.0
3+
= = 2.00
[Fe ] 10.0
Ecell = 0.511 V
c.
i. ∆ G° = - RT ln K sp
= 68.27 K J
∆ Go = - n F E o , n =1
E° = - 0.707 V
ii. Cu+ + I−  CuI(s) E° = 0.707 V
Cu2+ + e−  Cu+ E° = 0.153 V
The overall reaction for reduction of Cu2+ by I− is
Cu2+ + I− + e−  CuI(s) E° = 0.86 V
The E° value for the reduction of Cu2+ by I− can now be calculated

2 x Cu2+ + I− + e−  CuI(s) E° = 0.86 V
I2 + 2e−  2I− E° = 0.535 V

The over-all reaction is
2Cu2+ + 4I− → 2CuI(s) + I2 E° = 0.325 V
The positive value of effective E° indicates that the reduction reaction is

spontaneous. This has come about since in this reaction, I− is not only
a reducing agent, but is also a precipitating agent. Precipitation of Cu+
as CuI is the key step of the reaction, as it practically removes the
product Cu+ from the solution, driving the reaction in the forward
direction.
iii. ∆ Go = - n F Eo
Here n = 1, E o = 0.325 V
∆ G o = - 31.3 kJ
∆ G o = - RT ln K
log K = 5.47
K = 2.9 × 10 5
10. Solubility of sparingly soluble salts
a. Ag2C2O4 (s)  2 Ag+ + C2O42-
The solubility product Ksp is given by
Ksp = [Ag+]2 [C2O42−]
If S is the solubility of Ag2C2O4
[Ag+] = 2S (1)
The total oxalate concentration, denoted by Cox, is
Cox = S = [C2O42−−] + [HC2O4−] + [H2C2O4] (2)
The dissociation reactions are:
H2C2O4  H+ + HC2O4− K1 = 5.6 × 10−2 (3)
HC2O4-  H+ + C2O42−− K2 = 6.2 × 10−5 (4)

Eqs. (2), (3) and (4) give
2- [C 2 O24-][H+] [C 2 O 24− ][H + ] 2

Cox = S = [C2 O ] + 4 +
K2 K 1K 2
∴ [C2 O 24-] = α C ox = α S
K 1K 2
where α = + 2
(5)
[H ] + K1 [H+ ] + K1K 2
At pH = 7, [H+] =10−7 and α ≅ 1
Ksp = 4S3 = 3.5× 10−11
At pH = 5.0, [H+] = 10−5
From the values of K1, K2 and [H+] , we get
α = 0.861 (6)
Ksp = [2S]2 [αS]
1
 K sp  3
∴ S =   = 2.17 x 10- 4
 4α 
b. [NH3] = 0.002
At pH = 10.8, [H+] = 1.585 × 10-11
Eq. (5) implies
α=1
i.e Cox = S = [C2O4-2] (7)
The total silver ion in the solution is given by
CAg = 2 S = [Ag+] + [AgNH3+] + [Ag(NH3)2+] (8)

The complex formation reactions are
Ag+ + NH3  AgNH3+ K3 = 1.59 × 103 (9)
AgNH3+ + NH3  Ag(NH3)2+ K4 = 6.76 × 103 (10)
From eqs. (8), (9) and (10)
CAg = 2S = [Ag+]{1 + K3[NH3] + K3K4[NH3]2}
∴ [Ag+] = β x CAg = β x 2S
1
where β =
1 + K 3 [NH3 ] + K 3 K 4 [NH3 ]2
Using the values of K3, K4 and [NH3],
β = 2.31 x 10-4
2
K sp = [ Ag+] [C2 O24-]
= [β × 2S ]2 [S]
1
K sp 3
∴ S = ( )
4 β2
= 5.47 x 10 -2
11. Spectrophotometry
a. Denote the molar absorptivity of MnO4− at 440 nm and 545 nm by ε1 and ε2

and that of Cr2O7− by ∈3 and ∈4 :
∈1 = 95 Lmol−1cm−1, ∈2 = 2350 Lmol−1cm−1
∈3 = 370 Lmol−1cm−1, ∈4 = 11 Lmol−1cm−1
The absorbance A is related to % transmittance T by

A = 2 - log T
From the values given for the sample solution
A440 = 2 - log 35.5 = 0.45
A545 = 2 - log 16.6 = 0.78

Now if one denotes the molar concentrations of MnO4- and Cr2O72- in the steel
sample solution by C1 and C2 respectively, we have
A440 = ∈1 x C1 x 1 + ∈3 X C2 x 1
A545 = ∈2 x C1 x 1 + ∈4 X C2 x 1
Using the given data, we get
C1 = 0.0003266 M
C2 = 0.001132 M
Amount of Mn in 100 mL solution
= 0.0003266 molL-1 × 54.94 gmol-1 × 0.1 L
= 0.001794 g
0.001794 x 100
% Mn in steel sample = = 0.13%
1.374
Amount of Cr present in 100 mL solution
= 0.001132 mol L-1 x 2 x 52.00 g mol -1x 0.1 L
= 0.0118 g
0.0118 x 100
% Cr in steel sample = = 0.86%
1.374
b. In solution 1, since all the ligand is consumed in the formation of the complex,
2+ 2 x 10-5
[CoL ]
3 = = 0.667 x 10 − 5
3
Absorptivity of the complex CoL32+ is
0.203
∈ = −5
= 3.045 x 10 4 L mol-1cm-1
0.667 x 10 mol L-1 × 1.0 cm

If the concentration of the complex CoL32+ in solution 2 is C,
0.68
C =
3.045 x 10 L mol-1cm-1 x 1.0 cm
4
= 2.233 x 10-5 M
[Co2+] = [Co2+]total - [CoL32+]
= 3 x 10-5 - 2.233 x 10-5 = 0.767 x 10-5
Similarly, [L] = [L]total - 3[CoL32+]
= 7 x 10-5 - 3 x 2.233 x 10-5 = 0.300 ×10-5
The complex formation reaction is
Co2+ + 3L  [CoL32+]
The stability constant K is given by
[CoL23+ ]
K =
[Co2 + ][L]3
= 1.08 x 1017
12. Reactions in buffer medium
RNO2 + 4H+ + 4e → RNHOH + H2O

HOAc  H+ + OAc-
[H+ ] [OAc − ]
Ka =
[HOAc ]
i.e
[HOAc]
pK a = pH + log
[OAc - ]

4.76 = 5.0 + log

[HOAc ]
[OAc - ]
[HOAc]
= 0.5715
[OAc - ]
[HOAc] + [OAc - ] = 0.500
[OAc − ] = 0.3182
[HOAc] = 0.5 − 0.3182 = 0.1818
mmoles of acetate (OAc−) present initially in 300 mL
= 0.3182 x 300 = 95.45
mmoles of acetic acid (HOAc ) present initially in 300 mL
= 0.1818 x 300 = 54.55
mmoles of RNO2 reduced
= 300 x 0.0100 = 3
From the stoichiometry of the equation, 3 mmoles of RNO2 will consume 12

moles of H+ for reduction. The H+ is obtained from dissociation of HOAc.
On complete electrolytic reduction of RNO2,
mmoles of HOAc = 54.55 − 12.00 = 42.55
mmoles of OAc− = 95.45 + 12.00 = 107.45
42.55
4.76 = pH + log
107.45
pH = 5.16

13. Identification of an inorganic compound
a. The white gelatinous precipitate in group (III) obtained by qualitative analysis

of solution B indicates the presence of Al3+ ions. The white precipitate with
AgNO3 indicates the presence of Cl− ions.
From the above data the compound A must be a dimer of aluminium chloride
Al2Cl6.
b. The reactions are as follows

Al2Cl6 → 2[Al.6H2O]3 + + 6Cl-
H2 O
6Cl− + 6AgNO3 → 6AgCl(s) + 6NO3−
AgCl(s) + NH4 OH(aq) → Ag(NH3 ) + or Ag(NH3 ) +2 + H2 O + Cl-
+
Al3 + + NH4OH(aq) → Al(OH)3(s) + NH4
Al(OH)3(s) + NaOH(aq) → [Al(OH)4 ]- + Na+
[Al(OH) 4 ] - + CO 2 → Al(OH)3 ( s ) + HCO 3-
Al2Cl6 + LIH → (AlH3 )n  → Li[AlH4 ]

excess of LiH
14. Ionic and metallic structures
a. i. The lattice of NaCl consist of interpenetrating fcc lattices of Na+ and Cl-
ii. The co-ordination number of sodium is six since, it is surrounded by six

nearest chloride ions.

iii. For NaCl, the number of Na+ ions is: twelve at the edge centres shared
equally by four unit cells thereby effectively contributing 12 x 1/4 =
3Na+ ions per unit cell and one at body center. Thus, a total of 3 + 1 = 4
Na+ ions per unit cell.
Number of Cl- ions is: six at the center of the faces shared equally by
two unit cells, thereby effectively contributing 6 × 1/2 = 3 Cl- ions per
unit cell and eight at the corners of the unit cell shared equally by eight
unit cells thereby effectively contributing 8 × 1/8 = 1 Cl- ion per unit cell.
Thus, a total of 3+ 1 = 4 Cl- ions per unit cell.
Hence, the number of formula units of NaCl per unit cell = 4Na+ + 4Cl- =
4NaCl.
iv. The face diagonal of the cube is equal to √2 times 'a' the lattice
constant for NaCl type structure. The anions/anions touch each other
along the face diagonal. The anion/cations touch each other along the
cell edge.
Thus, a = 2 (r+ + r-) ……………..(1)
Face diagonal √2 a = 4 r- ……………..(2)
Substituting for 'a' from (1) into (2) we get :
√2 × 2 (r+ + r-) = 4 r- from which,
the limiting radius ratio r+ / r- = 0.414
v. The chloride ion array is expanded to make the octahedral holes large
enough to accommodate the sodium ions since, the rNa+/ rCl- ratio of
0.564 is larger than the ideal limiting value of 0.414 for octahedral six
coordination number.
vi. As the cation radius is progressively increased, the anions will no

longer touch each other and the structure becomes progressively less
stable. There is insufficient room for more anions till the cation / anion
radius ratio equals 0.732 when, eight anions can just be grouped

around the cation resulting in a cubic eight coordination number as in

CsCl.
vii. Generally, the fcc structure with a six coordination number is stable in
the cation/anion radius ratio range 0.414 to 0.732. That is, if 0.414 <
r+/r- < 0.732 then, the resulting ionic structure will generally be NaCl
type fcc.
b.
i. Bragg's law states λ = 2dhkl Sin(θ)
154 pm = 2 × d200Sin(15.8° )
154 pm 154 pm
d200 = °
= = 283 pm
2 × Sin(15.8 ) 2 × 0.272
Thus, the separation between the (200) planes of NaCl is 283 pm.
ii. Length of the unit cell edge, a = d100 = 2 × d200
a = 2 × 283pm = 566 pm.
iii. Since it is an fcc lattice,
cell edge, a = 2(rNa+ + rCl-)
radius of sodium ion r Na+ = a - 2 rCl- = 566 - 362 = 102 pm

2 2
c.
i. The difference in an hcp and a ccp arrangement is as follows:
The two 'A' layers in a hcp arrangement are oriented in the same
direction making the packing of successive layers ABAB.. and the
pattern repeats after the second layer whereas, they are oriented in the
opposite direction in a ccp arrangement resulting in a ABCABC…
packing pattern which repeats after the third layer.
The unit cell in a ccp arrangement is based on a cubic lattice whereas

in a hcp arrangement it is based on a hexagonal lattice.

ii. Packing fraction = Volume occupied by 4 atoms

Volume of unit cell
Let 'a' be the length of the unit cell edge

Since it is an fcc lattice, face diagonal = √2a = 4r ………..(1)
Volume of the unit cell = a3
4 × 4 π r3
Packing fraction = ...............................(2)
3 × a3
Substituting for ‘a’ from (1) into (2), we get
4 × 4 × 22 × ( 2 )3 × r 3
Packing fraction = = 0.74
3 × 7 × ( 4r ) 3
Thus, packing fraction in a ccp arrangement = 0.74
iii. The coordination number(12) and the packing fraction (0.74) remain
the same in a hcp as in a ccp arrangement.
d.
i. For an fcc structure, face diagonal = √2a = 4rNi
where a = lattice constant
rNi = radius of the nickel atom
rNi = √2 × a = √2 × 352.4 pm = 124.6pm

4 4
ii. Volume of unit cell = a3 = (3.524 Å)3 = 43.76Å3
iii. Density of Nickel, ρNi = Z×M/N

V
No. of Ni atoms, Z = 4 for an fcc unit cell
Avogadro constant
N= Z×M = 4 × 58.69 g mol-1

ρNi V 8.902 g cm-3 × 43.76 ×10 -24 cm3
N = 6.02 × 10 23 mol-1

15. Compounds of nitrogen
a.
i. NO2 : No. of electrons in the valence shell around nitrogen

=5+0+2 =7
The lewis structure for NO2 is as shown below.
.. . ..
:O: : N : O
.. :
According to VSEPR, the molecule ideally should have linear

geometry. However, this molecule has one single unpaired electron
present on nitrogen. Due to the repulsion between the unpaired
electron and the other two bonded pairs of electrons, the observed
bond angle is less than 180 (132o). Thus, the shape of the molecule is
angular as shown below.
O
. N
132o
ii. NO2+: No. of electrons in the valence shell around nitrogen

= (5 + 2 + 2 –1 ) = 8
The Lewis structure is as shown below
.. + ..
:O: : N : : O:
Thus, there are no non-bonded electrons present on nitrogen. The two

σ - bonds will prefer to stay at 180o to minimize repulsion between
bonded electron pairs giving a linear geometry (180o). The π-bonds do
not influence the shape.
+
O N O

NO2-: No. of electron in the valence shell around nitrogen

=5+2+1 =8
The Lewis structure is as shown below

O
.. .. .. -
:O: : N : O : : N 115 o
..
O-
In case of NO2-, there is a lone pair of electrons present on nitrogen.

Due to strong repulsion between the lone pair of electrons and the
bonded pairs of electrons the angle between the two bond pairs shrinks
from the ideal 120o to 115o.
b. In case of trimethylamine, the shape of the molecule is pyramidal with a lone

pair present on nitrogen. Due to the lone pair Me-N-Me angle is reduced from
109o4′ to 108°.
..
SiH3
N H3Si N
SiH3
Me Me
Me
However, in case of trisilylamine, d orbital of silicon and p orbital of nitrogen

overlaps giving double bond character to the N-Si bond. Thus, delocalisation
of the lone electron pair of nitrogen takes place and the resultant molecule is
planar with 120° bond angle.
N Si
empty d-orbital
filled p-orbital

c. Both N and B are tricovalent. However, NF3 is pyramidal in shape. In case of

BF3, the B-F bond gets double bond character due to the overlapping of p
orbitals present on boron and fluorine. The observed bond energy is, therefore,
much greater in BF3
..
F
N
B F
F
F F
F
filled p-orbital
empty
p-orbital
d.
i. The difference in boiling points of NF3 and NH3 is due to hydrogen

bonding which is present in ammonia.
High electronegativity of fluorine decreases the basicity of nitrogen in

NF3. Thus, NF3 does not act as a Lewis base.
ii. In NF3, the unshared pair of electrons contributes to a dipole moment in

the direction opposite to that of the net dipole moment of the
N-F bonds. See figure (a).
..
..
N N
F H
F H
F H
NF 3 NH 3
(a ) (b)

In NH3, the net dipole moment of the N-H bonds and the dipole moment
due to the unshared pair of electrons are in the same direction. See
figure (b).
e.
2 NaNO3 + 8 Na ( Hg ) + 4 H 2O → Na2 N 2O2 + 8 NaOH + 8Hg
NH 2OH + EtNO2 + 2 NaOEt → Na2 N 2O2 + 3EtOH
Na2N2O2 is the salt of H2N2O2 (Hyponitrous acid).
Structure :
.. OH
HO OH or
N N N N
.. .. HO ..
H O
N N
H O
Isomer is: H2N NO2 (Nitramide)
16. Structure elucidation with stereochemistry
a. H2C COOH H2C COOH

H2SO4
HO C COOH C O + H2O + CO
H2C COOH H2C COOH
3-oxo-1,3-pentanedioic acid
α - Hydroxy carboxylic acids undergo similar reaction.

b. Molecular weight of A = 236

20 mL 0.05 M KOH ≡ 118 mg A
1000 mL 1 M KOH ≡ 118 g A
∴ The acid is dibasic
Molecular weight of A = 236

80 mg Br2 ≡ 118 mg A
160 gm Br2 ≡ 236 g A
A contains one double bond
C C
It has anisole ring in the molecule
OCH3
It is formed from HOOC− CH2−CO−CH2−COOH

It has molecular formula C12H12O5
Due to steric hindrance the attachment of the aliphatic portion on the
anisole ring will be para with respect to -OCH3. Hence the structure will be
COOH
H3C O
COOH
As A forms anhydride the two COOH groups should be on the same side of
the double bond.
c. Isomers of A
OCH 3
COOH
COOH
( E ) 3-( 2-methoxyphenyl )-2-pentenedioic acid
CH3O COOH
COOH
( Z ) 3-( 2-methoxyphenyl )-2-pentenedioic acid

HOOC
CH3O
COOH
( Z ) 3-( 4-methoxyphenyl )-2-pentenedioic acid
d. Two products are possible when compound A reacts with bromine.
COOH COOH
H Br Br H
HOOC H2C Br Br CH2 COOH
OCH3
OCH3
[1] [2]
Structures 1 and 2 are enantiomers.
e. COOH COOH
S R
H Br Br H
R S
HOOC H2C Br Br C H 2 C OO H
OCH3 OC H 3
f. CH 2 COOH
O O Product obtained by reaction with phenol

B
CH2COOH
HO O O Product obtained by reaction with resorcinol

C
g. In the formation of compound A from anisole, the attack takes place at the p-
position of the OCH3 group. However, when compound B is formed from
phenol, the attack takes place at the o-position of the OH group.

Steric hindrance of OCH3 group favours the attack at the para position. Steric
hindrance of the OH group is less. Thus, the attack is possible at the ortho or
para positions. However, addition at ortho position is favoured as it leads to
cyclization of the intermediate acid to stable B.
h. Phenol has only one OH group on the phenyl ring whereas resorcinol has two
OH groups on the phenyl ring at the m-positions. Hence, position 4 is
considerably more activated (i.e, electron rich) in the case of resorcinol.
5
6 4
1 3
OH HO 2 OH
Phenol
Resorcinol
Therefore, under identical reaction conditions, the yield of compound C is

much higher than that of B.
17. Organic spectroscopy and structure determination
a. The given Molecular formula is C3H60. Therefore, the possible structures are:
H O
O H O CH3
H3C C C C C
C H
CH3 H H
H3C H
I III
II
H H
H O O C C
H H CH2 OH
CH3
H
V VI
IV
The NMR spectrum of compound A shows a single peak which indicates that
all the protons in A are equivalent. This holds true only for structure I. The
IUPAC name of this compound is 2-propanone.

The NMR spectrum of compound B shows four sets of peaks, which indicate
the presence of four non-equivalent protons. This holds true for structures III
and IV. However, for structure IV, no singlet peak (see peak at δ = 3) will be
observed. So, compound B must have structure III. The IUPAC name is 1-
methoxyethene.
b. Hb Ha
C C
Hc OCH3
Three doublets of doublets centred at 6.5 ppm, 3.9 ppm, 3.5 ppm are seen in
the spectrum. The assignments in the spectrum are
Ha : 6.5 ppm
Hb : 3.5 ppm
Hc : 3.9 ppm
Due to the presence of electron donating OCH3, the trans proton Hb has
higher electron density and thus more shielded than Hc. Thus, Hb appears
upfield as compared to Hc. There is also a singlet line at δ=3. This
corresponds to the H in OCH3.
c. Coupling constants
Ha : 12, 16 Hz J ( Ha, Hb) = 12 Hz

J ( Ha, Hc) = 16 Hz
Hb : 8, 12 Hz J ( Ha, Hb) = 12 Hz
J ( Hb, Hc) = 8 Hz
Hc : 8, 16 Hz J ( Hb, Hc) = 8 Hz
J ( Hc, Ha) = 16 Hz
Note: J = (difference in two lines in ppm) x (Instrument frequency)

Geminal coupling < cis-vicinal coupling < trans-vicinal coupling

d.
Peak positions in Hz Peak positions in Hz
(for 400 MHz instrument) (for 600 MHz instrument)
2614 3921
2602 3903
2598 3897
2586 3879
e. Compound A will react with malonic acid in the following manner
H3C COOH H3C O C

Addition
C O + H2C C CH2
H3C COOH H3C OH COOH
Compound A Malonic Acid
-H2O
O
H3C O C
C CH2
H3C O C
O
Meldrum's acid ( C6H8O4 )
The structure of Meldrum’s acid is consistent with the 1H-NMR and IR data.
The peak in the IR spectrum at 1700 –1800 cm-1 is because of the C=O
stretching. The presence of peaks only between 0 – 7 δ in the 1H-NMR
spectrum indicates that the compound doesn’t have any acidic group like
COOH or OH.
If compound B reacts, the only possibility is that it will add across the double
bond giving a product with molecular formula equal to C6H10O5. This
molecular formula does not match with the one stated in the problem.

H O OCH3
COOH
OCH3 + H2 C HOOC C C O C CH3
COOH
H H
Compound B Malonic Acid
f. The increased acidity is due to active –CH2 group of Meldrum's acid flanked
by two – CO groups. The carbanion formed at –CH2 will be stabilised by these
–CO groups, which are coplanar.
H3C O C
C CH2
H3C O C
O
M e ld r u m 's a c i d ( C 6 H 8 O 4 )
g. The condensation product of Meldrum's acid with an aromatic aldehyde has

the structure
O
O
O Ar
O
18. Polymer synthesis
Ag cat
a. H2C CH2 + 1/2 O2 H2C CH2
250O C
Ethylene O
P
+
H2C CH2 H OH
+ H2O HO
O Q
b. H2C CH2 OH O
+ HO HO OH
O
P Q R

O
SOCl2 O
HO OH Cl Cl
R S
O alc. KOH O
Cl Cl
S T
c.
COOH COOCH3
CH3 CH2 CH2

CH2Br CH2CN
+
NBS KCN H / H2O / CH3OH /
peroxide EtOH/H2O or i) NaOH / H2O H+
CCl4 +
ii) H / H2O
CH2Br CH2CN CH2 CH2
CH3
COOH COOCH3
p-xylene
dimethyl benzene-1,4-bis(acetate)
d. Three signals (three singlets for -CH3, –CH2 and aromatic protons)
e. Structure of polymer
CH3O C CH2 CH2 C O CH2 CH2 O CH2 CH2 O H
O
n
I) KOH / H2O /
f. O
Polymer + HOOC CH2 CH2 COOH + HO OH
II) H / H2O
LiAlH4 O
Polymer HO CH2 CH2 CH2 CH2 OH + HO OH
g. With Glycerol (being a triol), cross-links between the polymer chains involving
the secondary hydroxyl group will form a three-dimensional network polymer.

H2C OH
HC OH
H2C OH
Glycerol
O H O
CH2 CH2 C O CH2 C CH2 O C CH2
C O
CH2
CH2
C O
The polymer is unsuitable for drawing fibers because of its Cross-linked,

resin-like property.
19. Organic synthesis involving regioselection
a. The product obtained in the presence of catalyst HSbF6 is m-bromophenol.

From the mass spectra given in the problem, direct bromination of phenol
gives o/p–bromo derivatives as OH group present in phenol is o/p- directing.
OH OH OCH 3 OCH 3
b.
HSbF 6 ( Cat ) ( CH 3 ) 2 SO 4 Mg / THF / toluene
Br 2 NaOH
Br Br MgBr
Phenol A B C
Compound B may undergo nucleophilic reaction at the carbon bearing

bromine. Compound C contains a carbanion and hence functions as a
nucleophile and will attack an electrophile. Thus, reactivity of B is reversed on
its conversion to C (umpolung).

c. O O
CH3
CH2O N
CH3
CH3
HN
CH3 D
Cyclohexanone
OCH3
OCH3 O
CH3
+ N OH
CH3 CH3
MgBr N
CH3
C D
Tramadol
d. PhOCH3
HO
HO PhOCH3
H
CH2 N(CH3)2
CH2 N(CH3)2
H
PhOCH3 HO PhOCH3
HO CH2 N(CH3)2
H
H
CH2 N(CH3)2
Tramadol has two asymmetric carbon atoms. It has two pairs of enantiomers .
20. Carbon acids
a. The molecular formula of the keto ester is C5H8O3. Since X and Y are keto
esters, they must have the following units-
O O
keto group ester group
C C C O C
This accounts for C4O3 .The remaining part comprises of CH8. Thus, only two
types of ester groups are possible, methyl or ethyl.

For a methyl ester: CH3 will be a part of the ester moiety. This leaves CH5 to
be attached.
For an ethyl ester: CH2CH3 will be a part of the ester group. Therefore H3 unit
needs to be accounted for.
Therefore, possible structures of the keto esters are:
O O O O
H3C CH2 C C OCH3 H3C C CH2 C OCH3
Structure I Structure II
O O
H 3C C C O CH2 CH3
Structure III
b. Reaction sequence for keto esters
O O O O
NaOCH3
CH2 C O CH3 H3C CH C C OCH3
* H3C C
PhCH2Br
CH2Ph
Structure I
Keto acid ( C12H14O3 )
CH3 O O CH3 O O
+
LDA ( 1equiv. ) H / H2O
H3C C C C O CH3 H3C C C C OH
CH3I
CH2Ph CH2Ph

O O O O
NaOCH3
H3C C C O CH2 CH3 H2C C C O CH2 CH3
* PhCH2Br
Structure Ill CH2Ph
CH3 O O CH3 O O
+
LDA ( 1equiv. ) H / H2O
HC C C O CH2 CH3 HC C C OH
CH3I
CH2Ph CH2Ph

O O
H3C C CH2 C OCH3 Structure ll
NaOMe PhCH2Br
O O
LDA ( 2 equiv. ) LDA ( 1 equvi. ) / MeI
H3C C CH C OCH3
MeI
CH2Ph
O O O CH3 O
H2C C CH C OCH3 H3C C C C OCH3
CH2Ph
CH3 CH2Ph
+
+ H / H2
H / H2
O CH3 O
O H O
H3C C C C OH
H2C C C C OH
CH2Ph
CH3 CH2Ph
l - Keto acid
B
B
l - Keto acid
-CO2
-CO2
O CH3
O
H3C C C H
H2C C CH2 CH2 Ph
CH2Ph
CH3
( C11H14O ) ( C11H14O )
♦ Structure I gives a keto acid with molecular formula C12H14O3 which

matches with the formula of the keto acid obtained from Y.
∴ Structure I is Y.
♦ Structure II gives a neutral compound with molecular formula C11H14O that
matches with the molecular formula of the neutral acid stated for X.
∴ Structure II is X.
♦ Structure III gives a keto acid with molecular formula C11H12O3 that also
does not match with any given molecular formula.

Hence the two keto esters are :
O O O O
CH 3 CH 2 C C OCH 3 CH 3 C CH 2 C OCH 3
Compound Y Compound X
(Structure I) (Structure II)
α-keto ester β-keto ester
c. The β-keto ester gives on hydrolysis a β-keto acid. This acid readily
undergoes decarboxylation involving a 6-membered transition state, giving a
neutral product ( Ketone ).
H O H
O O
H3C CH2 C C CH2Ph + CO2
H2C C C
H H
C O
CH3
CH2Ph
H2C C CH2
CH3 CH2Ph
d. i. When 1 equivalent of LDA is used compound X produces a carbanion

(monoanion) as shown below.
O H O O O
LDA ( 1 equiv. ) -
H3C C C C OCH3 H 3C C C C OCH3
CH2Ph
CH2Ph
Carbanion
Compound X ( monoanion )
ii. Use of 2 equivalents of LDA leads to the formation of a dianion .
O H O O O
LDA ( 2 equiv. ) - -
H3C C C C OCH3 H2C C C C OCH3
CH2Ph
CH2Ph
Compound X Dianion

21. Amino acids and enzymes
a. The protonated amino group has an electron withdrawing effect. This

enhances the release of proton from the neighboring –COOH, by stabilizing
the conjugate base –COO-. This effect is greater when the –COO- is
physically closer to −NH3+. As −NH3+ group is present on the α-carbon, the
effect is greater on α-COOH than on the γ-COOH. So the pKa value of α-
COOH is lower than that of γ-COOH.
b. The ratio of ionized to unionized γ-COOH group is obtained by using

Henderson-Hasselbalch equation,
[COO − ]
pH = pK a + log
[COOH]
The pH = 6.3 and pKa of γ-COOH group is 4.3. Substituting these values in
the above equation we get,
[COO − ]
6.3 = 4.3 + log
[COOH]
100
∴ [COOH] = = 0.99% at pH 6.3
101
c. Glutamic acid has two pKa values lower than 7.0 and one pKa value higher
than 7.0. Thus, the isoelectric point (pI) for glutamic acid will lie between the
two acidic pKa values.
pI = (2.2 + 4.3)/ 2 = 3.25
At pH = 3.25, net charge on glutamic acid will be zero since this pH coincides
with pI of glutamic acid. Hence, glutamic acid will be stationary at pH 3.25.

d. In the hydrolysis of the glycosidic bond, the glycosidic bridge oxygen goes with
C4 of the sugar B. On cleavage, 18O from water will be found on C1 of sugar A.
O
B O
A O
C1 C4 O
n
H218O
O
18 B O
A OH HO
+ C4 O
C1
NOTE: The reaction proceeds with a carbonium ion stabilized on the C1 of

sugar A.
e. Most glycosidases contain two carboxylates at the active site that are
catalytically important. Lysozyme is active only when one carboxylate is
protonated and the other is deprotonated. A descending limb on the alkaline
side of the pH profile is due to ionization of -COOH. An ascending limb on the
acidic side is due to protonation of -COO−. Thus the enzyme activity drops
sharply on either side of the optimum pH. The ideal state of ionization at pH =
5 will be,
Lysozyme
(Asp-52) (Glu-35)
-
COO COOH

NOTE: It is desirable to study the amino acid side chains (R-groups) and their
ionization properties. The pKa values of these groups significantly determine
the pH dependence of enzyme activity.
f. Answers 2 and 4 are correct. Ionization of −COOH leads to generation of a

negatively charged species, −COO−. This charged species is poorly stabilized
by diminished polarity and enhanced negative charge. Hence ionization of
−COOH group is suppressed and the pKa is elevated.
g. The ratios of pseudo-first order rate constant (at 1M CH3COO−) in (a) to the
first order rate constants in (b) and (c) provide the effective local
concentrations.
For example, (2) (0.4) / (0.002) = 200
i.e the effective concentration = 200 M
(3) (20) / (0.002) = 10,000
i.e the effective concentration = 10,000 M
h. In addition to the enhanced local concentration effect, the COO− group in (3)
is better oriented to act in catalysis. The double bond restricts the motion of
COO− and thus reduces the number of unsuitable orientation of −COO−,
thereby enhancing the reaction rate.
22. Coenzyme chemistry
a. Step 1: Schiff base formation
H
-
H3C COO
N:
H CHO
-
H3C COO
+
+ + H2O
NH3

Step 2: Proton abstraction
:B
H -
- H3C COO H3C
-
H3 C COO (-) COO
N: N: N:
Base
(-)
Step 3: Reprotonation
- H* -
H 3C (-) COO COO
H 3C
N: N:
BH*
Step 4: Hydrolysis
H -
H3C COO
N: CHO
H -
H3C COO
+ + +
H2 O NH3
b. From the information stated in the problem, the following conclusions can be
drawn:
Structure 2: Removal of the phosphate group does not hamper the activity.
This indicates that the phosphate is not critical for the activity of
PLP.

Similarly,
Structure 3: CH2 -OH is not critical.
Structure 4: Phenolic OH is needed in the free form.
Structure 5: NO2, a well-known electron withdrawing group, causes

benzaldehyde to become activated. Hence positively charged
nitrogen in structure 3 must be also important for its electron
withdrawing effect.
Structure 6: Electron withdrawing effect of NO2 is only effective from the para
position. Introduction of this group at meta position leads to an
inactive analog.
c. Role of metal ion: The metal ion is involved in a chelation, as shown below,
and provides an explanation for the critical role of the phenolic OH. The planar
structure formed due to chelation assists in the electron flow.
H3C -
O
N +
M
O
H
+N
H
d. Step 1: Schiff base formation and decarboxlyation
O
- -
OOC - OOC
O
N: N:
.. + CO2
+N N
H H

Step 2: Tautomerization
- + -
OOC H OOC
N: N:
..
N N
+H
H
Step 3: Hydrolysis
-
OOC
N: CHO
-
OOC
+ H 2O +
NH2 +N
+N H
H GABA
e. Step 1: Schiff base formation followed by carbon- carbon bond scission.

H H
- -
COO COO
B H O
N N
H
+
.. O H
+N N
H H (X)
Step 2: Tautomerization followed by hydrolysis

+ -
H COO
N
- CHO
COO
+ H 2O + +
.. NH3
N N
H H

23. Protein folding
a. The planar amide group, that is, Cα, O, H and the next Cα are in a single plane
- is stabilized by resonance. The C-N bond of the amide assumes partial
double bond character and the overlap between p orbitals of O, C and N is
maximized. The Cα’s across this partial double bond can assume cis or trans
arrangement.
C C
.. H + H
N N
O C O- C
C H
N
O C
b. With nineteen of the amino acids, the trans arrangement is sterically favoured
(i. e. it is comparatively less crowded). In the case of proline, cis and trans
arrangements are almost equally crowded.
H C H C
N N
C O O C
trans – amide cis - amide
C C C C
N N
C O O C
trans – amide cis - amide

c. Note about Ramchandran diagram: In a polypeptide, the amide units are

planar (partial double bond character across the N-C bond) but the bonds
connecting N and Cα, and the carbonyl carbon and Cα are free to rotate.
These rotational angles are defined as φ and ψ, respectively. The
conformation of the main chain is completely defined by these angles. Only
some combinations of these angles are allowed while others are disallowed
due to steric hindrance. The allowed ranges of φ and ψ angles are visualised
as a steric contour diagram, shown below, known as the Ramachandran
diagram.
For nineteen amino acids, the conformational choice is largely restricted to the
so-called α and β regions on left half of the Ramachandran diagram (Panel
A). This is due to the L - chiral nature of amino acids and the steric effects of
their R groups. Glycine is an achiral residue with H as the R group. Therefore,
much larger conformational regions on both left and right halves of
Ramachandran diagram are accessible to this residue (Panel B).
Panel A Panel B
d. Consecutive residues in α conformation form the α-helix. Similarly,

consecutive residues in β conformation form the β-sheet. Both α-helix and β-
sheet structures feature extensive networks of hydrogen bonds which stabilise
them. Thus random combinations of α and β conformations are rarely found.

α - helix
β - sheet
e. For a polypeptide to fold in an aqueous environment, nearly half the R groups

should be nonpolar (water hating) and the other half polar (water loving).
Upon folding to form a globular protein, the nonpolar R groups are packed
inside (away from water) while the polar groups are positioned on the surface
(in contact with water). The phenomenon is similar to the hydrophobic
aggregation of a micellar structure in water. If all the R groups are either polar
or non-polar, no hydrophobic segregation is possible, and no folding will
occur.
f. Alternating polar/nonpolar periodicity of R groups favors β-sheets. All the non-

polar groups will face the apolar surface while the polar groups will be
exposed to water. So the net folding will be like a β-sheet. On the other hand,
a complex periodic pattern of R group polarities is needed in forming the α-
helix.

Hydrophobic Apolar Induced

periodicity + surface ⇒ (secondary
(primary (interface) structure)
sequence)
24. Protein sequencing
The sequence of amino acids in a protein or polypeptide is expressed starting from

the N-terminal amino acid. From Edman degradation method the N-terminal amino
acid is Asp. In the N-terminal fragment generated by trypsin or CNBr this amino acid
should, therefore, be in position1. All other peptides generated by CNBr cleavage will
be preceded by Met on their N-terminal side. Likewise, all peptides generated by
trypsin should be preceded by Arg or Lys. As we proceed from N-terminal amino
acid to C-terminal amino acid, we carefully examine the different amino acids in each
position shown in Table1(a) and 1(b)

For the first fragment starting from N-terminal Asp in position 1, we look for residues
common in each position to CNBr and trypsin cleaved peptides. This gives
Position 1 2 3 4 5 6
Residue Asp -Pro/Tyr - Tyr -Val -Ile/Leu -Arg …..(1)
At position 6 Arg will render the polypeptide susceptible to trypsin. Therefore, 7th
residue of this CNBr fragment (Table1a) should be same as residue1 in another
peptide generated by trypsin and 8th residue of this CNBr fragment will be same as
residue 2 in Table 1(b). Therefore we get
7 8
Gly/Phe - Tyr …..(2)
Since 8 will be Tyr, Pro will be assigned to position 2 of the polypeptide …..(3)
Residue 9 in the polypeptide should be at position 3 in the Table1(b) and residues

10,11,12,13 and 14 should be at positions 4,5,6,7 and 8 respectively in Table1(b).
The same residues should be in positions 1 onwards in Table1(a).
None of the residues in position 3 (Table1b) is same as in position 1 in Table 1(a).

However, positions 4 to 8 in Table 1(b) have residues common with positions 1 to 5
in Table 1(a). Further Glu in position 1 (Table 1a) will be preceded by Met (since it is
a part of CNBr cleaved peptide). And position 3 in Table 1(b) has Met. Therefore,
we get
9 10 11 12 13 14
Met- Glu - Thr - Ser - Ilu - Leu …..(4)
Position 5 in the polypeptide can now be firmly assigned to Ilu …..(5)
Positions 15 and 16 in the polypeptide will be beyond residue 8 in the trypsin cleaved
peptide (not shown here). We now attempt to construct the remaining trypsin or
CNBr fragments.

Table 1 (a) shows Arg in position 1. This will be preceded by a Met. Matching of the
unassigned residues in position 2 in Table 1(a) with those in position 1 in Table 1(b)
and for subsequent positions by the procedure demonstrated earlier that will give.
Met - Arg - Tyr - Pro - His - Asn - Trp - Phe - Lys - Gly - Cys …..(6)
(The last two residues are the unassigned residues in position 1 and 2 in Table 1b)
Considering (2), (5) and (6) together it is now possible to firmly assign position 7 on
the polypeptide to Gly …..(7)
a. The amino acid sequence common to the first fragments (N-terminal)

obtained by CNBr and trypsin treatments is
1 2 3 4 5
Asp - Pro - Tyr - Val - Ile
b. The sequence of the first fragment generated by CNBr treatment is
1 2 3 4 5 6 7 8
Asp- Pro - Tyr- Val- Ile -Arg -Gly -Tyr
To complete the sequence of the polypeptide we need to construct the sequence of

another trypsin fragment. Starting from position 4-(Arg) in Table 1(a) we get the
sequence,
Arg-Phe-His-Thr-Ala ..... (8)
At this stage, we again examine the unassigned residues. The Arg in (8) will have to
be serially preceded by Asn, Gln, Gly and Met (these are the unassigned residues in
respective positions in Table 1(a). We then get the sequence,
Met-Gly-Gln-Asn-Arg-Phe-His-Thr-Ala …..(9)
And following the Ala in (9)
Leu-Ser-Cys-Glu … ..(10)
From (9) and (10), we get the sequence

Met-Gly-Gln-Asn-Arg-Phe-His-Thr-Ala-Leu-Ser-Cys-Glu …..(11)
Since the smallest fragment is a dipeptide (Table 1b) and (6) shows that it follows
Lys, it follows that this will be at the C-terminal end. Therefore, the partial sequence
shown in (6) will follow the partial sequence shown in (11).Thus, we get
Met-Gly-Gln-Asn-Arg-Phe-His-Thr-Ala-Leu-Ser-Cys-Glu-Met-Arg-Tyr-Pro-His-Asn-
Trp-Phe-Lys-Gly-Cys …..(12)
There is already a Met in position 9 of the polypeptide. The next Met can only come
earliest at position 17 since CNBr fragment have at least 8 amino acids. Therefore,
the starting residues of (12) can be assigned position 17.
This leaves positions 15 and 16 which will be filled by the unassigned residues Val
and Ala in the CNBr fragment at positions 6 and 7 (Table 1a).
c. The final sequence, therefore, will be
Trypsin CNBr
1 2 3 4 5 6 ↓ 7 8 9 ↓ 10 11
Asp - Pro - Tyr - Val - Ile - Arg - Gly - Tyr - Met - Glu - Thr
CNBr Trypsin
12 13 14 15 16 17 ↓ 18 19 20 21 ↓ 22
Ser - Ile - Leu - Val - Ala - Met - Gly - Gln - Asn - Arg - Phe
CNBr Trypsin
23 24 25 26 27 28 29 30 ↓ 31 ↓ 32 33
His - Thr - Ala - Leu - Ser - Cys - Glu - Met - Arg - Tyr - Pro
Trypsin
34 35 36 37 38 ↓ 39 40
His - Asn - Trp - Phe - Lys - Gly - Cys
↓) indicate the CNBr and trypsin-labile sites.

Arrows (↓
d. There are 6 basic amino acid residues in the polypeptide. 6/40 = 15%
e. An α helix has 3.6 amino acid residues per turn of 5.4Å.

Thus, the length of the polypeptide in α helical conformation will be :
40/3.6 × 5.4 = 59.4 Å.
f. The polypeptide has 40 amino acids. Since each amino acid is coded for by a
triplet of nucleotides, the total number of nucleotide pairs in the double
stranded DNA of the exon will be
40 x 3 = 120 base pairs.
The molecular weight of the DNA making the exon
= 330 x 2 x 120
= 79200 D
g. If the exon contains 120 base pairs and A and C are in equal numbers, there
will be 60 A-T pairs and 60 G-C pairs. Each A-T pair is held by two H-bonds
and each G-C pair is held by three H-bonds. Hence the total number of H-
bonds holding this double helix is :
( 60 x 2 ) + ( 60 x 3 ) = 300

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33rd International Chemistry Olympiad ∗ Preparatory Problems

33rd International Chemistry Olympiad

Edited by Savita Ladage and Arvind Kumar

Copyright  2001 Homi Bhabha Centre for Science Education

Printed in Mumbai, India.

Homi Bhabha Centre for Science Education

Mumbai, India, July 2001

From the 33rd IChO Secretariat iv

Draft Syllabus for the International Chemistry Olympiad vii-xvi

Theoretical Problems 1-36

Practical Problems 37-48

Problem 25 Determination of aspirin in the given sample

Worked Solutions to Problems 49-111

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33rd IChO National Scientific Committee

Prof. N. Sathyamurthy Indian Institute of Technology, Kanpur

Prof. K. D. Deodhar Indian Institute of Technology, Mumbai

Supporting Scientific Staff

Mumbai, India, July 2001

SYLLABUS OF THE INTERNATIONAL CHEMISTRY OLYMPIAD

Level 1: These topics are included in the overwhelming majority of secondary

Level 2: These topics are included in a substantial number of secondary school

1 INORGANIC CHEMISTRY 1.4 Structures

1.1 Electronic configuration of atoms 1.4.1 simple molecular structures 2

1.2 Trends in the periodic table 1.5.1 oxidation number 1

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1.8 Natural cycles oxides with water and

1.9.1 Products of reactions of group I 1.11 d-Block

pressure, mole fraction) 3 2.4.10 Arrhenius equation, activation

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2.7.8 liquid-vapour system (diagram) 3 3.5 Arenes and heterocycles

3. ORGANIC CHEMISTRY 3.6 Halogen compounds

3.1 Alkanes 3.6.1 hydrolytic reactions 2

3.4.1 linear geometry 1 3.8.4 Reaction of carbonyl compounds

3.8.4.5 addition of NH2OH 2 3.11.6 mechanism of Hoffmann

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4.2.5 details of alpha-helix structure 3 4.5.13 detailed Calvin cycle 3

4.3 Fatty acids and fats 4.7.1 pyrimidine, purine 2

OTHER PROBLEMS 8. Instrumental methods of determining

7.1 energy levels of hydrogen atom 8.5 X-rays

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Syllabus for the Experimental Part of the IChO Competition

Level 1 is assigned to the basic experimental activities which are supposed to

1. Synthesis of inorganic and 1.24 washing of precipitates by

rod, Co-glass) 2 3.11 other types of determinations on basis

4.1 measuring with a pH-meter 2

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Values of Some Fundamental Constants

Avogadro number NA = 6.022 x 1023 mol-1

Faraday constant F = 96485 C mol-1

Gas constant R = 8.314 J. K-1. mol-1

Planck’s constant h = 6.626 x 10-34 J.s

Mass of electron me = 9.110 x 10-31 kg

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Water, the commonest substance around us, is an excellent system to understand

0 0.01 100 374

b. What is the effect of decrease of pressure on boiling point of water and

d. What is the phase of water at T = 300 K, P = 12.0 bar; T = 270 K, P = 1.00

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