BSc Biochemistry 2020 2023 Effective From June 2020

St.
Xavier’s College (Autonomous), Ahmedabad-9

BSc. Biochemistry
(Academic Year 2020-2023)
Programme Outcomes
PO1. Create a strong knowledge domain/ expertise
PO2. Develop critical thinking, Problem solving and research aptitude
PO3. Skill development
PO4. Encouraging social interaction, service learning and develop equity centred national
development (Social Extension work)
PO5. Self-directed and lifelong learning
PO6. Developing employability and entrepreneurial skills
PO7. Promoting Ecological sustainability development
PO8. Nurturing creativity and humane values
Programme Specific Outcome for BSc Biochemistry
PSO1. Describe the nature and basic concepts of all subjects that collate to applicability of
Biochemistry.
PSO2. Analyse biochemical systems, such as, changes associated with stressful conditions,
evolutionarily conserved pathways, genetic, nutritional and environmental adaptations
etc, and link it with life in all forms,
PSO3. Learn technical skills through laboratory sessions/ research projects and develop self-
directed experiential learning
PSO4. Ability to communicate the understanding of the learning to others
PSO5. Extend the applicability of Biochemistry to service learning and nation development
through awareness programmes/ action - oriented projects in health, nutrition, and
environment
Semester I
CORE Paper: Fundamentals of Biochemistry

Course Code: BC 1501
No. of Credits: 04
Learning Hours: 60 hrs
I. Course Outcome
The main objective of the course will be to build the basic foundation for studying biochemistry.
By the end of the paper, a student should be able to:
CO 1: To explain the importance of having water as a solvent system in cells
CO 2: To spell out the importance of bonding and spatial arrangements of molecules for proper
functioning and stability.
CO 3: To establish the concept of how proper conformations are needed for optimum
functioning of the molecules and thereby the entire cell
CO 4: To specify how proteins, carbohydrates, lipids and nucleic acids can contribute to
structural integrity of the cell as well as the biochemical reactions.
CO 5: To analyse how a change in the structure of the molecules can lead to abnormalities, for
eg. A mutated globin results in sickle cell anaemia
CO 6: To state both the physical as well as chemical properties of these biomolecules, as these
properties can be used to carry out various studies.
CO 7: Appreciate experiments carried out by scientists to enable understand the structure of
biomolecules, understand their properties, design of experiments to prove the same and
analyse the data and give interpretations.
Thus, the knowledge from this course can help in the following:
a. The students could pursue a career in clinical Biochemistry as maintaining levels of these
biomolecules in the body are of utmost importance. The decrease or increase in the
amount of some of the biomolecules can have clinical significance. For example,
increased blood sugar levels are indicative of a person suffering from diabetes mellitus.
b. The students can carry out basic research in Biochemistry, which in turn can be of great
help in the medical and diagnostic fields.
c. Students can also go in for Medical Laboratory Technique Courses, opening
opportunities in hospitals and pathological laboratories.
d. Basic knowledge of biochemistry is also required for Nutrition and Dietetics.
e. The understanding of proteins, its study, has opened up the field of Proteomics.
f. Many of the carbohydrates, proteins and lipids discussed have commercial value and
thus, find a place in Industrial Biotechnology.
II. Course Content
Unit 1: Chemistry of life: An introduction
B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 2

What is biochemistry, development of biochemistry, what is biochemical approach, scope of
biochemistry, applications of biochemistry, Biochemical literature (how to conduct a literature
search and how to read a research article).
Water: Properties of water, Water a biological solvent, Proton mobility, fitness of the aqueous
environment for living organisms, self-ionisation of water: Kw and pKw. Acid base reactions,
pH, pOH, pKa, weak and strong acids, physiological importance of pH; Osmosis and Donnan
membrane equilibrium.
Buffers: Buffers, buffer action, buffer capacity, Henderson – Hasselbalch equation, its
limitations and uses, laboratory use of buffers, physiological importance of buffers in body fluids
and tissues.
Measurement of pH: indicators, pH meter, different types of electrodes, advantages and

disadvantages of different electrodes, principle, working, application, factors affecting pH
determination
Chemical bonding (covalent, ionic, Hydrogen, Van der Waal’s, hydrophobic).
Unit 2: Carbohydrates
Introduction, natural occurrence and physiological importance; Classification and structure of
carbohydrates: aldose and ketoses, Mono, oligo and polysaccharides, Structure of
monosaccharide.
Configuration in sugars, reference carbohydrate, Fischer’s projection formula and representation

of various sugars, Haworth’s representation of cyclic structure. Furanose and pyranose structures
and representation of various sugars, Mutarotation, Conformation in sugars: boat and chair
forms.
Oligosaccharides – Occurrence, structure, chemical name, function and importance of maltose,

sucrose, lactose, cellobiose, trehalose, raffinose.
Polysaccharides – Occurrence, structure, chemical name, functions and importance of starch,

glycogen, cellulose, hemicellulose, dextrin, chitin, inulin, dextran, pectin, agar, alginic acid,
mannans.

Carbohydrate derivatives of biological importance: Amino sugars, deoxysugars, sugar
phosphates, blood group polysaccharides, cell wall polysaccharides, teichoic acids, muramic
acids, sialic acid, mucopeptides.
Glycobiology: Glycosaminoglycans - Occurrence, structures and functions of hyaluronic acid,

heparin, chondroitin sulphates (A, B and C), glycoproteins and proteoglycans, glycolipids.
Unit 3: Amino acids and Proteins

Introduction, structure and classification of standard amino acids, introduction to rare amino
acids, non-protein amino acids, essential vs Non-essential amino acids, Amino acids as
ampholytes and its stereoisomerism.
Chemical reactions of amino acids: Sanger’s reaction, Edman’s reaction, Nitrous acid reaction,
Siegfried’s carbamino reaction, Dansyl chloride reaction, oxidative deamination by oxides and
ninhydrin.
Proteins: Peptides – structure, formation and characteristics of peptide bond; Classification based
on solubility, shape and composition; Functions of proteins; Properties – isoelectric pH ,
hydration, behaviour in solution, solubility, salting in and salting out, precipitation of proteins by
acid reagents, heavy metals, heat, extreme pH changes, denaturation and renaturation of proteins.
Structure of proteins – primary, secondary, super secondary, tertiary and quaternary structures;
Determination of sequences of proteins (Protein sequencing); Biological functions of fibrous
proteins, keratins, collagen, elastin, globular proteins – haemoglobin, myoglobin, glycoproteins,
lipoproteins, nucleoproteins and metalloproteins.
Unit 4: Lipids
Lipids: Introduction, classification of lipids, fatty acids. Structure, properties, functions and
importance of saturated, unsaturated, hydroxyl, cyclic, branched chain fatty acids and PUFA;
Physical properties, isomerism, geometrical isomerism, positional isomers, melting point, boiling
point, solubility and absorption spectra; Chemical properties: salt formation, detergent,
esterification, hydrogenation, halogenations, oxidation, saponification; Chemical constants of
fats: saponification value, iodine number, Reichert Meissl number, acetyl number, acid number.
Rancidity of fats due to hydrolysis, oxidation and lipolysis, prevention of rancidity; Waxes –
natural waxes, properties and importance.
Complex lipids and Sterols: Glycerophospholipids – classification, properties and functions of

lecithin, lysolecithin, cephalins, plasmalogens, phosphatidyl serine, phosphatidyl inositol;

Sphingolipids: Classification, properties and functions of cerebrosides, gangliosides;
Sulpholipids, gangliosides, proteolipids and prostaglandins;
Structure and properties of sterols; Colour reactions of cholesterol.

Practical Paper: Fundamentals of Biochemistry
Course Code: BC 1502L
No. of Credits: 03
Session: 2 hours
I. Course Outcome
The main objective of the course will be to build the basic foundation as well as skill in the
subject of biochemistry.
CO 1: To explain the importance of various instruments used in biochemistry.
CO 2: To establish the concept with lab sessions
CO 3: To analyse and to identify carbohydrates
CO 4: To experimentally prove both the physical as well as chemical properties of these
biomolecules, as these properties can be used to carry out various studies.
CO 5: Appreciate experiments carried out by scientists to enable understand the structure of
biomolecules, understand their properties, design of experiments to prove the same and
analyse the data and give interpretations.
Note:
 Students should learn the principles, theory, protocol and calculations for each
experiment.
 They should learn about reagent preparations.
Basic Practicals
1. Introduction to Biochemistry Lab: Understanding of Lab Protocols. Safety aspects in
Biochemical Laboratory.
2. Glossary of technical terms in Biochemistry
3. Calibration of instruments and pipettes.
4. Biochemical reagent preparations for various solutions with respect to different
Normality, Molarity, % Solutions (W/V), (V/V).
5. Use of microscope and microscopic examination of osazones.
6. Preparation of distilled water.
7. pH measurements*& numerical based on pH & buffer.
8. Preparation of buffer and its pH determination.
Titration Practicals
8. Use of potassium dichromate in the standardization of sodium thiosulphate
9. Estimation of sugar by Cole’s method.

10. Water analysis for Hardness*.
Qualitative analysis
11. Qualitative tests for carbohydrates.
*Note: These will be conducted as a mini project, wherein the students will be asked to check
the pH and hardness of different water samples to conclude whether there is a correlation
between the two measured parameters and also discuss the results obtained.
III. Teaching methodologies: Apart from the conventional black board teaching, other modes of
teaching that will be adopted are power points, problem solving, and group projects.
Assignments will be designed such that students inculcate the habit of reading reference books
and science journals. The use of smart boards for teaching will also be promoted to enable more
interaction based teaching.
Emphasis will be given to systematic designing of experiments in the laboratory sessions.
IV. Recommended Learning Resources
1. Biochemistry, 5th Edition. Garrett and Grisham

2. Biochemistry, 3rd Edition. Matthews, van Holde, and Ahern
3. Biochemistry. 7th edition. Berg JM, Tymoczko JL, Stryer L. New York: W H Freeman;
2014
4. Lodish et al. Molecular Cell Biology. 8th Edition. W. H. Freeman and Company.
5. Textbook of Biochemistry with Clinical Correlations, 7th Edition by T. Devlin
6. Voet, D. and Voet, J.G. (2012) : Biochemistry 4th ed., ( John Wiley & Sons Inc/, New
York)
7. Harpers Review of Biochemistry, 25th Edition. Murray RK, Rodwell VW.
8. Lehninger’s Principles of Biochemistry, Nelson and Cox (2012) : Principles of
Biochemistry (Worth Publ. Inc. USA)
9. Concepts in Biochemistry, 3rd Edition. Rodney Boyer
10. http://en.wikibooks.org/wiki/Biochemistry
11. Introduction to Practical Biochemistry. T. Plummer.
12. Biochemistry, 4th Edition. U. Satyanarayana and U. Chakrapani. Elsevier; 2013

Semester II
CORE Paper: Concepts in Cell Biology
No. of Credits: 04
I. Course Outcome
The basic unit of life is a cell. Therefore, study of its structure and functions gives an insight into
an intricately woven network of efficient and coordinated molecular mechanisms that renders a
cell fit to not just survive but also to multiply, get differentiated and move around.
Understanding various concepts like how cells originated, transport across membranes, transport
within cells, cell division, regulation of cell cycle, cell senescence etc. opens up a lot of target
areas for drugs and treatment. For example, today there are a lot of drugs that target the
ribosomes, which has been possible because its structure and functions has been thoroughly
studied.
The course will give a detailed description of
a) The assembly of biomolecules to form a cell, which has been the crux of origin of life and the
evolutionary changes thereafter, especially, the role of RNA and genetic changes.
b) The detailed study of membrane biochemistry, transport across membranes and within cells by
cytoskeleton
c) Studying the organization of the cell and the structure and functions of various organelles.
d) The structure and function of nucleus, cell division, cell cycle regulation and senescence
By the end of the paper, a student should be able to
CO 1: To explain the evolution of a cell and the role of nucleic acids in evolution
CO 2: To describe the importance of semi permeable nature of plasma membrane in maintaining

the integrity of a cell.
CO 3: To establish the concept of how proper conformations of lipids and proteins in a

membrane are needed for optimum functioning
CO 4: To clarify how important each organelle is to make cell the basic unit of life – the entire
organization within a cell is a perfect example of division of labour with proper
coordination and networking.

CO 5: To demonstrate how a change in the structure of the molecules can lead to abnormalities,
for eg. Improper glucose transporter can affect blood sugar homeostasis
CO 6: To question why a cell cycle needs to be regulated and when does a cell need to die.
CO 7: Appreciate experiments carried out by scientists to enable understand the working of a

cell, design of experiments to prove the same and analyse the data and give
interpretations.
a) Research in elucidation of molecular mechanisms within a cell
b) Research in cancer biology, tissue engineering, stem cells etc.
c) Drug discovery targeting various anomalies due to malfunction of organelles
II. Course Content
Unit 1: Nucleic acids and Origin of Life

Introduction to nucleic acids, Composition of DNA and RNA. Nitrogenous bases: structure and
properties of normal and rare. Sugars. Nomenclature for writing the structure of nucleic acids.
Nucleosides and nucleotides: linkages, different types, naturally occurring, functions.
DNA: Important features of double helix structure.
RNA: Different types, structures, functions and differences and similarities with DNA.
Porphyrins: Introduction, nucleus, classifications, metalloporphyrins.

Origin of life: Living matter, early history, Chemical evolution, Origin of living systems
(molecules to first cell), RNA world, development of metabolic pathways, Central dogma of life,
mutation and evolution. Biological evolution: prokaryotes to eukaryotes; Differences between
plant and animal cells; Types of cells.
Unit 2: Structural components of cell

Membrane structure: Singer – Nicholson’s Fluid Mosaic Model, Structure and functions of
membrane lipids and glycolipids – membrane fluidity and movement, lipid rafts.
Membrane proteins: structure and types; principles of membrane transport, Carrier proteins and
active membrane transport, Ion channels
Membrane carbohydrates: Glycocalyx
Cytoskeleton: Nature of cytoskeleton, Intermediate filaments, Microtubules, Cilia and flagella,
Actin filaments; Molecular motors associated with cytoskeleton

Unit 3: Cell Organelles
Detailed structure and functions of: Mitochondria and Chloroplast (Energy Conversions) and the
Endosymbiont Theory, Endoplasmic reticulum: Rough and Smooth, Golgi apparatus,
Ribosomes, Lysosomes, Peroxisomes, Nucleus; Endomembrane network system and its
importance.
Unit 4: Cell cycle and Cell Senescence

Cell Cycle: General strategy of cell cycle, Interphase (Different stages) and Mitosis; Generation
time; Cell cycle regulation.
The Mechanics of Cell division; Introduction, an overview of different stages in Mitosis, meiosis
and cytokinesis.
Cell Senescence: Difference between aging and necrosis; Programmed Cell Death.
Practical Paper: Fundamentals of Biochemistry

No. of Credits: 03
Session: 2 hours
I. Course Outcome
CO 1: To explain the importance of various biomolecules and correlate concepts with lab
sessions
CO 2: To analyse and to identify proteins and lipids
CO 3: Appreciate experiments carried out by scientists to enable understand the working of a
cell, design of experiments to prove the same and analyse the data and give
interpretations.
Note:
 Students should know the principles, theory, protocol and calculations for each
experiments.
 They should know about reagent preparations.
Experiments involving titrations
1. Estimation of amino acid by formal titration

2. Use of potassium permanganate in the estimation of Iron.
3. Use of potassium permanganate in the estimation of Oxalate.
4. Use of potassium permanganate in the estimation of Nitrite.

5. Estimation of Calcium from biological fluid. (Serum)
Experiments based on lipids.

6. Determination of Acid number of edible oil.
7. Determination of saponification number of edible oil.
8. Estimation of unsaturated fat by iodine value of oil.
Experiments involving Qualitative Analysis

9. Qualitative analysis by colour reactions of Amino Acids.
10. Qualitative analysis of proteins gelatin, egg albumin by colour reactions and their
identification with the help of colour reactions.
11. Precipitation/ denaturation test for proteins by
a. Heat
b. pH (conc. HCl, 5/10 N NaOH, Distilled water)
c. Acids (TCA and Sulphosalicylic acid).
d. Heavy metals (Lead, Copper, Zinc, Barium Salts)
12. Analysis of physical property of lipids: Solubility test.
13. Analysis of chemical properties of lipids: colour reactions of cholesterol.
Experiments involving Colorimetric Estimations

14. Use of single cell colorimeter, its construction and operation. (Demo).
15. Estimation of protein by Biuret method.
16. Estimation of DNA by DPA method.
17. Estimation of RNA by Orcinol method.
18. Estimation of Sugars by DNSA method*
18. Permanent slides of

A. Different stages of cell division
a) Prophase
b) Metaphase
c) Anaphase
d) Cytokinesis
B. Different cell types
a) Epithelium
b) Endothelium
c) Muscle cells
d) Nerve cell
*Note: This will be conducted as a mini project, wherein the students will be asked to check
the sugar content of juices, soft drinks etc. and assess whether the sugar content is in
accordance to the amount written on their labels.

interaction based teaching. Videos from American Society of Cell Biology could also be shown
to students to imbibe concepts.
IV. Recommended learning Resources
1. Molecular Cell Biology, 7th Edition. Lodish, et. al.

2. Biochemistry, 4th edition. Donald Voet and Voet Judith
3. Harpers review of Biochemistry, 25th Edition. Murray RK, Rodwell VW.
4. Lehninger’s Principles of Biochemistry, 5th Edition. Nelson DL and Cox MM
5. Biochemistry, 5th Edition. Garrett and Grisham
6. Origin of life on the earth and in the cosmos (2nded), Geoffrey Zubay:Academic Press
7. Molecular Biology of the Cell, 5th Edition, Bruce Alberts et. al.
8. Organelle structure and function, David E Sadava, Jones Bartlett publishers.
9. Cytology, P.S. Verma, V.K. Agarval, S. Chand Publications.
10. Cell and Molecular Biology, 8th Edition. De Robertis.
11. Cell and Molecular Biology, Sheeler and Bianchi
12. The Cell: A Molecular Approach, 6th Edition, G.M. Cooper
13. Introduction to Practical Biochemistry. T. Plummer.
14. Practical Biochemistry - Satyanarayan
Semester- III
CORE Paper: Concepts in Microbiology
No. of Credits: 04
I. Course Outcome
CO 1: To explain the morphology of a prokaryotic cell and the fine structure of its organelles
CO 2: To differentiate between eubacteria, archaebacteria, fungi, algae and viruses and

comprehend their economic importance.
CO 3: To justify the discovery and advancement of microscopic techniques has led to

revolutionizing the field of microbiology
CO 4: To describe the basic growth requirements of bacteria in vitro in order to culture them.
CO 5: To know methodologies to control the growth of microbes by various sterilization

techniques and chemotherapeutic drugs. For example: Milk is pasteurized to ensure that
its shelf life is long; keeping surgical tools and rooms free of pathogens etc.

CO 6: To defend that good bacteria play a major role in industries especially food industries
CO 7: To justify how microbes have been a tool to minimise use of chemicals, improvise waste
water treatment and decreasing environmental pollution by biodegradation
CO 8: Appreciate experiments carried out by scientists to enable understand the use of microbial
systems in enhancing the quality of life.
a) The students could pursue a career in industries that specialize in synthesis of various
chemical components like acetic acid, enzymes, antibiotics, drugs etc.
b) The students can carry out basic research in Microbiology and Biotechnology, which in turn
can be of great help in the commercialization of various microbial products.
c) Students can also go in for Medical Laboratory Technique Courses, opening opportunities in
hospitals and pathological laboratories.
d) Basic knowledge of microbiology is required for Fermentation Technology which is a basic

technology used in many Pharmaceutical and Biotech companies.
e) Explore the field of genetic engineering
f) Entrepreneurial start ups for small scale industries like production of biofertilizers, fermented
foods etc.
II. Course Content
Unit 1: Basic structure of microbes

Cell morphology and fine structure of bacteria; Size, shape and arrangement of bacteria; study of
organelles: Structure, chemical composition and functions of – cell wall, cell membrane, flagella,
mesosomes, fimbriae and pilli, capsules, ribosomes, intracellular inclusions and endospores.
Identification of bacteria based on cell morphology and fine structure.
Salient features and economic importance of Archeabacteria, rickettsia, fungi, algae, and viruses
Unit 2: Microscopy
Parts of a compound microscope: condenser, objective, ocular lens systems; Basic principles of
image formation; Relationship between magnification and numerical aperture; angular power
and resolving power.

Principle, construction, working, limitations and applications of: dark-field microscopy, phase
contrast microscopy, fluorescent microscopy, Inverted microscopy and Electron (TEM, SEM)
microscopy.
Principle and applications of Confocal microscopy, AFM and Cryoelectric microscopy
Unit 3: Microbial growth, nutrition and control

Control of microorganisms: Definition of terms: sterilization, disinfection, microbicidal,
microbiostasis, sepsis and asepsis, antiseptic. Factors affecting; Sterilization and disinfection by
physical means: moist, dry heat, radiations and filtration; Sterilization and disinfection by
chemical means: characteristics of an ideal antimicrobial agent, phenol coefficient. Mode of
action and uses of: halogen and halogen compounds, compounds of heavy metals, phenols and
its derivatives, alcohol, detergents. Chemosterilant gases (formaldehyde, ethylene oxide, beta
propiolactone); Chemotherapeutic agents: Mode of action, limitations and uses of: penicillin,
streptomycin, tetracyclins, polymixins, choramphenicol, cephamines, sulfa drugs.
Growth and Nutrition: Definition and calculation of generation time, Growth curve, diauxic
growth curve. Measuring bacterial growth (SPC, serial dilution, direct microscopic count); Effect
of various factors on growth and reproduction of bacteria: temperature, osmotic pressure,
radiation, hydrostatic pressure, mechanical impact, surface tension (define types based on
specific requirement e.g. thermophilic); Cultivation of anaerobes, pure culture isolation and
preservation.
Nutritional requirements and broad categories of bacteria (auxotrophs, lithotrophsetc)
Preparation of media, Types of media (Natural, empirical, synthetic, defined, special media)
Unit 4: Applied Microbiology

Microbiology of Milk: pasteurization and sterilization, microbial analysis of milk (SPC, MBRT)
Role of microorganisms in fermented dairy products (butter, cheese, curd and yoghurt).
Microbiology of water and sewage: Definition of potable water, index organisms of fecal
contamination and their significance. Microbial analysis of water: SPC, filtration. MTFT, MPN.
Sewage microbiology: BOD and COD- definition and significance. Sewage treatments: Primary,
secondary (trickling filters, activated sludge process, oxidation ponds) and advanced treatments.
Solids processing. Biofertilizers: Bioremediation and phytoremediation, Soil microbiology.

1. Atlas R: Microbiology:Fundamentals and Applications (2nded)

2. Frobisher, Hinsdill, Crabtree, Goodheart: Fundamentals of Microbiology
3. Pelczar Reid: Microbiology (5thed)
4. Prescott: General Microbiology.
5. Scheeler and Bianchi: Cell Biology
6. Stainer, Adelber,Ingraham: General Microbiology
Semester- III
CORE Paper: Biophysical Chemistry
No. of Credits: 04
I. Course Outcome
CO 1: To state the basic concepts of physics like adsorption, viscosity, surface tension,
absorption of light to be able to apply in understanding concepts in biochemistry
CO 2: To correlate the use of a particular technique to understand a fundamental.
CO 3: To justify that the discovery and advancement of biophysics has opened up understanding
pathways and mode of actions of various biological systems.
CO 4: To apply the techniques for production, analysis and modifications of biomolecules.
CO 5: Design experiments with appropriate techniques in the methodologies and analyze the
data obtained.
a) The students could pursue a career in industries that specialize in Instrumentation specifically
for Life Science Research and Analysis
b) Avail jobs in Production, Quality Control and Rand D divisions of Pharmaceutical and
Biotech companies.

c) The students can carry out basic research in various areas of biology due to their
understanding of the techniques
d) Start up companies supplying basic instruments like colorimeters, pH meters, etc.
II. Course Content
Unit 1: Centrifugation and Viscosity

Poiseuille’s equation, unit of viscosity, relative viscosity and its determination, factors affecting
viscosity, physiological importance
Principle of sedimentation, factors affecting sedimentation
Types of rotors used in centrifuges, separation methods in different rotors
Preparative centrifuges: Differential centrifugation, sub cellular fractionation, density gradient
centrifugations; Applications, preparation of gradients, sample collection methods, zonal rotors
Analytical Centrifuges; Ultracentrifugation, working and applications
Unit 2: Adsorption, chromatography and electrophoresis

Principle of adsorption, orientation of molecules on a surface, factors affecting adsorption,
application of adsorption
Principle, technique, applications, advantages and disadvantages of: Ion exchange, gel filtration,
affinity chromatography. Adsorption chromatography. Thin layer chromatography, reverse phase
chromatography, hydrophobic interaction chromatography, HPLC, GLC.
Principle, technique, factors affecting, detection, applications, advantages and disadvantages of:
Gel electrophoresis (PAGE, agarose, starch gel), Isoelectric focusing, 2-D gel electrophoresis
Unit 3: Colorimeter and Spectroscopy

Beer-Lambert’s law, principle, working of single cell and double cell colorimeter.
Principle, working, applications, advantages and disadvantages of spectrophotometers and
spectrofluorimeters (expand in detail monochromators, light source)
Principle and applications of NMR, IR spectroscopy and atomic absorption spectroscopy
Unit 4: Advanced Techniques

Radioactive decay, units of radioactivity. Measurement of radioacitivity (Geiger Muller Counter,
scintillation counters, autoradiography). Applications of radioactivity and hazards.
Flow cytometry, Patch-clamp technique, Freeze fracture technique (Histology), ICP MS, GC
MS, LC MS.

II. Teaching methodologies: Apart from the conventional black board teaching, other modes of
1. Berg JM, and Tymoczko TJ, Stryer L,: Biochemistry (6th Ed)
2. Daniel, C Harris: Quantitative Chemical Analysis
3. David Freifelder: Physical biochemistry (2nd Ed) WH Freeman, USA)
4. Donald Voet and Voet J: Biochemistry (4th Ed) 2011
5. Ghatak KL: Techniques and methods in Biology. PHI learning Pvt Ltd. 2011
6. Nelson DL and Cox MM: Lehninger’s Principles of Biochemistry (5th Ed) 2008
7. Oser: Hawks Physiological Chemistry (4th Ed) 1965.
8. Upadhyay and Nath: Biophysical chemistry: Principles and Techniques (3rd Ed)
9. Van Holde KE: Physical Biochemistry. Prentice Hall, NJ.
10. Vogel AI: A text book of quantitative inorganic analysis (3rd Ed), 1975.
11. Westand Todd: Text book of biochemistry ((4th Ed) 1970
12. Wharton and McCarty: Experiments and methods in Biochemistry
13. Willard and Merrit: Instrumental methods of analysis (4th Ed) 1971.
14. Wilson K and Walker J: Principles and Techniques of Biochemistry and Molecular
Biology (6th Ed) 2006. Cambridge University Press.
Semester- III
Practical Paper: Fundamentals of Biophysical techniques and Microbiology
No. of Credits: 2.5
Session: 3 hours
I. Course Outcome
CO 1: Appreciate experiments carried out by scientists to enable understand the use of microbial
systems in enhancing the quality of life.
CO2: To apply the techniques for production, analysis and modifications of biomolecules.
CO3: Design experiments with appropriate techniques in the methodologies to study various
aspects of microorganisms

Note:
experiment.
Colorimetric Estimations
1. Estimation of sugar by Folin-Wu method
2. Estimation of protein by Folin-Lowry method
Biophysical methods
3. Measurement of absorption spectra
4. Agarose gel electrophoresis
5. SDS-Poly acrylamide gel electrophoresis
6. Thin layer chromatography
7. Paper chromatography
8. Column chromatography
9. Off site visit to Industry
Basic techniques in Microbiology

10. Introduction to stains and staining procedures
11. Monochrome staining( Positive and negative)
12. Gram staining
13. Capsule staining
14. Metachromatic granules staining
15. Spore staining(optional)
16. Methylene blue reduction test
17. Antibiotic assay by agar cup method
18. Antibiotic assay by disc/ditch method
19. Identification of microorganisms and Fermentation tests for microorganisms
20. Study of growth characteristics of microorganisms*
21. Alcohol fermentation by yeast*
*Note: These will be conducted as a mini project, wherein the students will be asked to check
the growth characteristics of microorganisms under static and aerated conditions; under
different temperature and pH conditions. Production of alcohol by yeasts from different food
sources.
References
1. Plummer: An introduction to practical Biochemistry
2. Thomas and Schalkhammer: Analytical Biochemistry, 2002
3. Varley H: Practical Clinical Biochemistry
4. Wharton and McCarty: Experimental methods in Biochemistry
5. Willard and Merrit: Instrumental methods of analysis.
6. Seeley HW and Van Denmark PJ: Microbes in Action

7. Wistreich GA and Lechman MD: Laboratory Exercise in Microbiology

Semester IV
CORE Paper: Molecular Physiology
No. of Credits: 04
I. Course Outcome
CO 1: To justify that physiological functions of cells are aided and regulated by signal
molecules likes hormones, owing to its specificity and transduction mechanisms, which
in turn become a target for treatment of various ailments
CO 2: To describe the molecular mechanisms involved in blood clotting, production of

erythrocytes, leucocytes and thrombocytes. This also gives an insight into molecular
mechanisms that could be induced to enhance production of cells in vitro.
CO 3: To explain the underlying mechanisms involved in movement of different muscle types

to facilitate specific functions.
CO 4: To state the importance of secretions and absorption in the body to aid digestion,
circulation and excretions. The mechanisms involved will also enable comprehend what
happens when there is any defect in any of the steps.
CO 5: Appreciate experiments carried out by scientists to enable understand the basic concepts
involved in signalling, transport, regulation and movement.
a) An ability to carry out basic research in understanding various physiological actions in cells.
b) Work in research institutions, hospitals which are involved in finding molecular targets to
treat diseases.
c) Opportunities to work in companies that are into discovery of drugs that target cells at the
molecular level for therapeutics
d) Work as skilled technicians in pathological laboratories, blood banks and hospitals.

II. Course Content
Unit 1: Hormone signalling mechanisms

Classification of hormones, Characteristics of hormones; Hormone receptors;
Mode of action of hormones: cAMP, calcium, IP3, DAG, receptor kinases, cGMP, NO and gene
activation; Regulation by feedback mechanisms e.g. Thyroid hormones, TSH and TRH;
Synthesis and regulation of Insulin, glucagon, thyroid hormone, estrogen, and growth hormone.
Unit 2: Circulatory and Respiratory System

Hematopoeisis: Erythropoesis, Thrombocyte formation and leucopoesis.
Hemostasis: Vasoconstrictions, Platelet plug formation, Clot – Clotting factors; intrinsic and
extrinsic pathways for blood clotting. Clot retraction.
Role of surface tension in inhalation; (Theory of surface tension and its measurement); Role of
hemoglobin in oxygen transport, dissociation curve of oxyhemoglobin and its significance.
Bohr’s effect, transport of oxygen and carbon dioxide, chloride shift.
Various buffer systems of the blood, acid base balance, factors affecting acid-base balance.
Acidosis and alkalosis, Role of lung and kidney in regulation of acid base balance.
Unit 3: Muscle movement in body systems

Excitation and contraction of muscles – molecular organization of muscle, proteins of
contractile element; their organization and role in contraction; Energy for contraction .
Theories of contraction; Hormonal regulation.
Cardiac physiology- circulation, electrophysiology of heart. Measurement of blood pressure,
hypo and hypertension.
Regulation of striated and smooth muscle movement in the GI tract for propulsion and mixing.
Unit 4: Secretions and Absorption

Salivary secretions and its regulation, gastric secretions and its regulation, pancreatic secretions
and its regulation; Biliary secretions and its regulation; Secretions of the small intestine and its
regulation; Absorption processes in the small intestine and large intestine; Transport of nutrients
after absorption; Examples of disorders due to anomalies in regulation.
Functions of glomerular membrane and glomerular filtration rate (GFR), selective reabsorption
and secretion, active passive transport of various substances (sugars, amino acids, urea and
creatinine), mechanism of urine formation; Role of hormones in regulation.

1. Best and Taylor: Physiological basis of Medical practice

2. Bhagavan NV: Medical Biochemistry (4thed), Jones and Bartlett Publishers
3. Charterjee: Human Physiology Vol. 1 and 2.
4. Chatterjee and Shinde: Text book of Medical Biochemistry
5. Das AK: Human Physiology
6. Ganong WF: Review of Medical Physiology (12thed). Lange Medical Publishers
7. Guyton AG and Hall JE: Text book of Medical Physiology (11thed) Harcourt Asia.
8. Murray RK, Granner DK, Mayes PA and Rodwell, VW: Harper’s Biochemistry (25thed)
2000, Prentice Hall publishers.
9. Sherwood: Human Physiology (5thed) 2004
10. Talwar PC: Text book of Biochemistry and Human Physiology
11. Tortora G and Derrickson B: Principles of Anatomy and Physiology (14thed) 2014. John
Wiley and sons.
12. Sembulingam K and Sembulingam P: Essentials of Medical Physiology (6th ed) 2012.
Jaypee Brothers Medical Publishers
Semester- IV
CORE Paper: Nutrition
No. of Credits: 04
I. Course Overview
The main objective of the course will be to understand the importance of Nutrition and its
biochemical implications
CO 1: To explain simple concepts related to Nutrition like balanced diet, RDA etc.,
CO 2: To correlate between food and energy requirements and utilization;

CO 3: To demonstrate why the body requires carbohydrates, lipids and proteins in specific
quantities and how its deficiency or excess can lead to disorders
CO 4: To assess the contribution of minerals, trace elements and vitamins to the well being of
humans.
CO 5: Appreciate experiments carried out by scientists to enable understand the requirement of

different molecules by the body
a) Enable students to build a career as a nutritionist
b) Find employment as dieticians in hospitals, health care agencies.
c) The students can carry out basic research in nutrition based projects
d) Start up companies supplying basic health supplements
II. Course Content
Unit 1: Introduction and Energy Metabolism

Introduction: Introduction to nutrition science: current trends in nutrition, nutrition in India:
RDA, balanced diet, assessment of nutritional status
Energy metabolism: Energy molecules, energy value of foods (gross and physiological fuel
value), units of energy; Determination of energy value of foods by direct and indirect
calorimetry; Determination of energy expenditure: direct and indirect methods, RQ and its
significance; Total energy requirements, factors affecting it. BMR: definition, measurements,
and factors affecting it; SDA of foods; Food habits of people and relate it to balanced nutrition
Unit 2: Nutritional and Physiological Functions of Carbohydrates, Proteins, Lipids

Carbohydrates: Nutritionally important carbohydrates, function of carbohydrates, carbohydrate
loading, lactose intolerance; Dietary fibres: role in human nutrition; Ethyl alcohol; Dental caries.
Lipids: Animal and vegetable lipids in diet; Fatty acids: essential fatty acids, PUFA/P/S ratio;
Fats: storage (adipose tissue), transport, mobilization, ketosis, function and requirements;
Obesity
Proteins: Source of dietary proteins, nitrogen balance; Quality of proteins: complete, incomplete
proteins, supplementary values, Indices: BV, NPU, PER, PDCASS, digestibility, NDpV.

Unit 3: Minerals and Trace Elements
Essentiality, classification and functions of minerals; Calcium, Phosphorus, iron, iodine,
selenium, zinc, fluorine.
Dietary sources; Absorption, transport, storage, excretion, malnutrition and toxicity of each of
the above.
Diseases associated with deficiency of minerals and trace elements
Unit 4: Vitamins
Water soluble vitamins: Occurrence/ Dietary sources; Biochemical functions; recommended
dietary allowances; assimilation; and deficiency.
Fat soluble vitamins: Occurrence/ Dietary sources; Biochemical functions; recommended dietary
allowances; assimilation and deficiency.
.
1. B. Srilakshmi: Dietetics
2. B. Srilakshmi: Nutrition Science
3. Christopher Haslett: Davidson’s principles and Practice of medicine (18thed) 1999.
Churchill Livingston.
4. Guthrie
5. Guyton A: Text book of Medical Physiology (10thed).
6. Murray H et al: Harper’s Biochemistry (25thed) 2000.
7. Rang HM and Dale MM: Rang and Dale’s pharmacology (6thed) 2007, Churchill
Livingston Elsevier.
Practical Paper: Nutrition and Heamatology

No. of Credits: 2.5

Session: 3 hours
I. Course Outcome
CO 1: Appreciate experiments carried out by scientists to enable understand the basic concepts
involved in signalling, transport, regulation and movement.
CO 2: To assess the contribution of minerals, trace elements and vitamins to the well being of
humans.
CO 3: Appreciate experiments carried out by scientists to enable understand the requirement of

different molecules by the body
Note:
experiment.
Nutrition
1. Estimation of Iron by KSCN method
2. Estimation of Magnesium
3. Estimation of Calcium
4. Estimation of Vitamin C*
5. Measurement of obesity indices*
6. Interpretation of Lipid Profile Indices*
7. Tests for Food adulteration*
Urine Analysis
8. Physical parameters of Urine
9. Normal chemical constituents of Urine
10. Detecting abnormal and pathological constituents of Urine
Basic Hematology
11. Red blood cell count
12. White blood cell count
13. Differential counting
14. Estimation of Hb by Sahli’s method
15. Determination of ESR
16. Determination of PCV
17. Determination of bleeding time, clotting time and blood group

*Note: These will be conducted as a mini project, wherein the students will be asked to,i)
determine the Vitamin C content from different food sources; ii) Comment on the obesity
indices of subjects of different age groups and correlate the same with lifestyle and diet;
iii)Analyze the lipid profile of various subjects; iv) Food adulterations as mini projects
References
1. Oser: Hawk’s Physiological Chemistry (14thed)
2. Plummer: An introduction to practical Biochemistry
3. Sheela Sharma: Experiments and Techniques, 2007.
5. Varlery H: Practical Clinical Biochemistry
6. Whatton and McCarty: Experimental methods in Biochemistry
Semester V
CORE Paper: Metabolism-I
No. of Credits: 04
I. Course Outcome
The main objective of the course will be to understand the concepts of Metabolism and its
importance in the proper functioning of each cell.
CO 1: To understand simple concepts related to metabolism,
CO 2: To see the correlation between energy molecules, reducing equivalents and pathways;
CO 3: To comprehend how metabolism is regulated by enzymes and hormones
CO 4: To compare anabolic and catabolic pathways of carbohydrates, proteins and nucleic acids
and comprehend how any defect in a pathway could lead to diseases.
CO 5: Appreciate experiments carried out by scientists to enable understand the pathways and
cycles of metabolism
a) Give a basic understanding of clinical aspects of biochemistry
b) Discover drugs related to metabolic disorders

c) Basic technical knowledge required in pathological laboratories
d) Work in industries related to diagnostics
e) Carry out basic research in understanding aspects of metabolism that are still not clear
II. Course Content
Unit 1: Introduction to Metabolism

Introduction to Metabolism, Terms, Overall view of Metabolism, general features of metabolism,
Chemical basis of high standard energy of hydrolysis of ATP, other phosphorylated compounds
and thioesters, NAD and NADH, common regulatory mechanisms in metabolic pathways,
genetic control of enzyme synthesis, regulation of the activity of enzymes, Hormones and
regulatory cascades, difference between anabolic and catabolic pathways, Experimental
Approach to Metabolism.
Unit 2: Metabolism of Carbohydrates

Glycolysis, energetics, regulation of glycolysis, fates of pyruvate, Feeder pathways, Glycogen
degradation, Glycogen synthesis, Regulation of glycogen metabolism, difference between
glycogenolysis and glycogenesis, glycogen storage diseases, Gluconeogenesis, reciprocal
regulation of Glycolysis & Gluconeogenesis, difference between Glycolysis & Gluconeogenesis,
Cori cycle, Alternate pathways, PPP and regulation and significance.
Unit 3: Metabolism of Proteins

Over view of the fate of carbon skeletons of amino acids, Gamma-Glutamyl cycle,
Transamination, oxidative deamination, Non-oxidative, glucose alanine shuttle decarboxylation,
Urea cycle , its regulation, energetics, and significance; Uric acid formation, Creatine
metabolism, Disorders of amino acids metabolism, cell surface glycoproteins and membrane
skeleton proteins
Porphyrin biosynthesis, catabolism and disorders of porphyrin metabolism.
Unit 4: Metabolism of Nucleic acids

Digestion of nucleic acids, degradation of purine and pyrimidine nucleotides. Inhibitors of
nucleotide metabolism, Disorders of purine and pyrimidine metabolism: Lesch-Nyhan
syndrome, Gout, SCID, adenosine deaminase deficiency.

1. Berg JM, and Tymoczko TJ Stryer L,: Biochemistry (7thed), (2012).WH Freeman
Publishers
2. Bhagvan NV: Medical Biochemistry (4thed) Bartlett Publishers.
3. Donald Voet and Voet J: Biochemistry (4thed) 2011, Wiley Publications.
4. Grisham and Garett: Biochemistry (3rded), Pearson-Thomson publishers
5. Jeoffrey Zubay: Principles of Biochemistry, McGraw Hill Publications, (1996).
6. Murray RK, Rodwell VW: Harpers review of Biochemistry (25thed), (2000).
7. Nelson DL and Cox MM: Lehninger’s Principles of Biochemistry (7thed) 2017.
8. Metzler: Biochemistry (2nded)
9. Dee Unglaub Silverthron: Human Physiology an integrated approach (5thed), Pearson –
Benjamin Cummngs (2010).
CORE Paper: Molecular Biology-I

No. of Credits: 04
I. Course Outcome
The main objective of the course will be to understand the importance of Molecular Biology and
its implications.
CO1: To analyse the experiments carried out by various scientists to prove that DNA is the
genetic material,
CO2: To explain the structure and properties of DNA;
CO3: To narrate the mechanisms of DNA replication, transcription and translation in prokaryotes
CO4: To evaluate how DNA damage can lead to detrimental effects and how DNA repair
systems in the cells try to prevent mutations before being inherited.
CO5: To outline how cells regulate expression of genes during transcription

CO6: Appreciate experiments carried out by scientists to enable understand the Central Dogma
of life
a) Enable students to build a career in Genetic engineering, Genomics and proteomics
b) Understanding of molecular mechanisms can enable customizing treatments related to

diseases
c) The students can carry out basic research in cell and molecular biology
d) Start up companies based on biologics and molecular medicines.
II. Course Content
Unit 1: Basic Concepts in Molecular Biology

Introduction to Molecular Biology; Experiments proving DNA as genetic material: S. F.
Griffith’s transforming principle, Avery, McLeod and McCarthy’s experiment, Roger Heriot’s
experiments with bacteriophages and Hershey and Chase Experiment; Rosalind Franklin’s
studies with DNA structure; Chargaff’s experiments and Law; Watson – Crick Model;
Deviations from Watson – Crick’s DNA model; Different forms of DNA;
Physical properties of DNA: Denaturation and Hyperchromic effect, Tm and its significance,
Renaturation and hypochromic effect, Cot Curve and its significance; DNA Supercoiling and
Topology
Unit 2: DNA Replication, DNA Damage and its Repair

Introduction to DNA replication; Messelson – Stahl’s experiment; the basic requirements of
DNA replication: Template – primer junction, DNA Polymerases: Structure and Function,
Ancillary proteins associated with replication; Mechanism of replication: Initiation, Elongation
and Termination; other modes of replication: Rolling circle mechanism and D – loop mechanism.
Mutations and Types of Mutations; Replication Errors and its Repair; DNA Damage by
Chemical Mutagens; DNA damage by physical agents; DNA Repair Mechanisms: Direct
Reversal of DNA Damage, Base excision repair and Nucleotide excision repair.
Unit 3: Genetic Code and Transcription

The Genetic Code: Cracking of the code and its triplet nature; Degeneracy and Universality;
Initiation and Stop Codons; Wobble’s Hypothesis and its significance.
Introduction to Transcription; RNA polymerase: structure and function; Promoters; Transcription
Initiation; Transcription elongation and proof reading: Termination of transcription.

Post transcriptional modifications: 5’ capping and poly A tailing; RNA splicing: Chemistry of
RNA splicing, Spliceosome machinery, Splicing pathways; Concept of Alternate Splicing.
Unit 4: Translation and Regulation of Gene Expression

Introduction to Translation, Roles of messenger RNA, transfer RNA, Aminoacyl tRNA
synthetases, and Ribosomes; Mechanism: Initiation of translation, Elongation and Termination;
Post translation modifications.
Regulation of Gene Expression: Principles; Regulation of transcriptional initiation: Lac Operon,
Arabinose Operon and Tryptophan Operon; Gene Regulation after transcription initiation.
1. Berg JM, and Tymoczko TJ, Stryer L,: Biochemistry (6th Edition)
2. Watson, J.D - Molecular Biology of the Gene (5th Edition)
3. De Robertis and De Robertis: Cell and Molecular Biology (8th Edition)
4. Donald Voet and Voet J: Biochemistry (4th Edition) 2011
5. Grisham and Garett: Biochemistry (3rd ed)
6. Benjamin Lewin: Genes IX (2007)
7. Nelson DL and Cox MM: Lehninger’s Principles of Biochemistry (7th ed) 2017
8. Lodish: Molecular Cell Biology (5th Edition) 2004
CORE Paper: Enzymology

No. of Credits: 04
I. Course Outcome

CO1: To describe the structures and functions of enzymes and its classification
CO2: Relate the parameters associated with enzyme activity
CO3: To outline mechanisms of catalysis and the involvement of various cofactors and
coenzymes in the process;
CO4: To know concepts on how to purify a protein using various techniques
CO5: To reason out how the rate of reaction of an enzyme is affected by physical and chemical
factors
CO6: To differentiate between regulatory enzymes and non regulatory enzymes through kinetic
studies
CO7: Appreciate experiments carried out by scientists to enable understand the pathways and
a. Use concepts of purification of enzymes in industries

b. Study different molecules that can modify enzyme activity
c. Gain basic technical knowledge required in laboratories
d. Work in industries related to enzymes
e. Carry out basic research in purifying and characterizing enzymes to establish an application
in industry or research
II. Course Content
Unit 1: Introduction
History, general characteristics, nomenclature, IUB enzyme classification, significance of
numbering system. Definitions with examples; holoenzyme, apoenzyme, cofactors, coenzymes,
activators, inhibitors.
Units of enzyme activity, Definition of IU, Katal, enzyme turn over number abd specific activity.
Metallo-enzymes, isoenzymes, monomeric and oligomeric enzymes and multi-enzyme

complexes.
Unit 2: Enzyme catalysis

Role of cofactors in enzyme catalysis: NAD/NADP, FMN/FAD, coenzyme A, biotin, cobamine,
TPP, pyridoxal phosphate, terahydoxy folate.

Acid-base catalysis, covalent catalysis, proximity and orientation effects, strain and distortion
theory. Mechanism of action of chymotrypsin, carboxypeptidase and lysozyme.
Enzyme specificity and active-site.
Unit 3: Enzyme Purification

Need for purification and general outline of purification scheme, Purification table, methods for
protein determination, purification methods with respect to source, principle, isolation and
extraction method, efficiency with examples and advantages or disadvantages during use.
Methods to check enzyme purity such as ultracentrifugation, electrophoresis & solubility.
Methodology, sampling & continuous methods with examples, advantages,disadvantages of: (a)
Spectrophotometric method (b) Spectrofluorometric method(c) Electrochemical methods (d)
Polarimetric method, and(e) Manometric method;Handling of enzymes, Enzyme assays.
Unit 4: Enzyme Kinetics
Factors affecting enzyme activity: enzyme concentration, substrate concentration, pH and

temperature.
Derivation of Michaelis-Menten equation for uni-substrate reactions. Km and its significance.

Line Weaver-Burk plot, Eadie - Hoofstie Plot and Hanes plot. Bi-substrate reactions - brief
introduction to sequential and ping-pong mechanism with examples.
Kinetics of zero and first order reactions; Significance and evaluation of energy of activation and
free energy.
Reversible and irreversible inhibition, competitive, non-competitive and un-competitive

inhibition, determination of Km and Vmax in presence and absence of inhibitors. Allosteric
enzymes – regulation and kinetics.

1. M. Dixon, E. C. Webb, C.J.R Thorne and K.F. Tipton (1979) Enzymes. 3rd Edition,
Longmans, Green & Co., London, and Academic Press, New York.
2. Price NC and Stevens L: Fundamentals of Enzymology, (1999) 3rd Edition, Oxford
University Press, USA
3. Foster R L: The nature of enzymology, Wiley (1980)
4. Palmer T: Understanding Enzymes (1995), 4th Edition, Ellis Horwood Ltd
5. Palmer T: Enzymes: Biochemistry, Biotechnology and Clinical Chemistry, Horwood
Series (2001)
6. Conn and Stumpf: Outlines of Biochemistry (2009), 5th Edition, John Wiley and Sons
7. Nelson DL and Cox MM: Lehninger’s Principles of Biochemistry (2014), 6th Edition, W.
H. Freeman
CORE Paper: Applied Biochemistry

No. of Credits: 04
I. Course Outcome
The main objective of the course will be to understand the applications of metabolic reactions,
enzymes and fermentation
CO1: To demonstrate how understanding of biochemistry of various processes enable applying

to diagnostics, analysis and therapy,
CO2: To appraise how enzymes are used at an industrial level;
CO3: To prove how simple fermentation processes yield economically important products
CO4: To develop upstream and downstream processing
CO5: To study various products obtained by fermentation
CO6: Appreciate experiments carried out by scientists to enable practical applications of theory
a) Give a basic understanding of clinical aspects of biochemistry and its use in diagnosis
c) Start small scale industries using microbes and enzymes
d) Work in industries related to fermentation
II. Course Content
Unit 1: Clinical Biochemistry

Biochemical tests in clinical medicine: uses; criteria for selecting a method for biochemical
analysis; enzymes as diagnostic tool; isoenzymes and their diagnostic importance; methods for
the detection of isoenzymes; organ function tests: clinical presentation and diagnosis of the
diseases of liver and kidney; bilirubin metabolism and hyperbilirubinaemia; acid base disorders.
Use of glucose oxidase in enzyme electrodes.
Tumour markers, Bone markers, Cardiac markers, liver markers.
Unit 2: Industrial application of enzymes

Immobilization of enzymes and their applications; Production of glucose from starch, cellulose
and dextran; Use of lactase in dairy industry; Production of glucose-fructose syrup from sucrose;
Use of proteases in food, detergent and leather industry.
Unit 3: Fermentation Technology

Introduction to fermentation; Types of fermentation products: Biomass, Microbial enzymes,
metabolites, recombinant products and transformation processes; Upstream Processing: Media
for industrial fermentation- carbon source, nitrogen source, micronutrients, oxygen requirement;
Sterilization- types and methods; inoculum development; Downstream processing-harvesting
cells, product recovery-extracellular and intracellular.
Unit 4: Fermentation in Industry

Products of microbial origin: citric acid, glutamic acid, lysine, alcohol, protease, lipase,
pectinase, xanthan.
Products of algal origin: Carragenan, asthaxanthin, anti-coagulants, anti HIV compounds.
Microorganisms as source of nutrition, energy and fuel.
1. Stanbury P., Whitaker and Hall. Principles of Fermentation Technology. Second Edition

2. Palmer T: UnderstandingEnzymes. Horwood Publishers. 2001
3. Muray-Moo Young. Comprehensive Biotechnology. Elsevier. 2004
4. Allan Gaw et al. Clinical Biochemistry (5th ed). Elsevier. 2013
5. Simon Walker et al. Clinical Biochemistry (9th ed). Wiley-Blackwell. 2013
6. William J. Marshall. Clinical Biochemistry: Metabolic and Clinical Aspects (3rd ed).
Elsevier. 2014
7. Victor W. Rodwell et al. Harper’s Illustrated Biochemistry (30th ed). Mc Graw Hill
Education. 2015
Subject Elective Paper: Research methodology and Biostatistics.

No. of Credits: 02
I. Course Outcome
The main objective of the course will be to build the basic foundation for doing research and to
give general overview of the field of intellectual properties. It explains the importance of
planning and development in research, designing and implementation of methodology to
maintain quality of research.
It explains the concepts and rational behind data analysis. Students will be introduced to basic
statistical methods to help prove hypotheses and validate data.
CO1: To develop most appropriate research strategy.
CO2: Know and use different methods and strategy for research.
CO3: To explain basic concepts of statistics and its application in biology
CO 4: To collect sample, categorize the data and understand variables
CO 5: Use measurements of central tendencies, deviation and errors
CO 6: To Analyse and interpret experimental results
CO 7: To solve problems involving Permutations, Combinations and Probability
CO 8: Use simple statistics softwares for substantiating data
a) The students can carry out quality research in Biochemistry, which in turn can be of great help
to the society.
b) The students are able to carry out significant research.
c) The students could pursue a career in Biostatistics
II. Course Content
Unit 1: Research methodology: an introduction

Meaning of research, objectives of research, types of research, research approaches, significance
of research, research methods versus methodology, research process and criteria of good
research.
Defining research problem, selecting the problem, necessity of defining the problem, technique
involved in defining a problem. Ethics in research: Honesty and integrity, Misconducts:
Falsification, fabrication, plagiarism. Best/ standard practices and guidelines.
Unit 2: Research Designs, interpretation and report writing

Research designs: Meaning of research designs, need for research designs, features of good
designs, and important concepts of good designs, differential research designs, and basic
principles of experimental designs.
Interpretation and report writing: Meaning and need to interpret, techniques of interpretation,
precaution in interpretation. Significance of report writing, Layout and types of report,
precautions for writing reports. Redundant publication: duplication and overlapping of
publications, selective reporting and misinterpretation of data. Conflict of interest, Violation of
publication ethics: authorship and contributorship.
Unit 3: Basic concepts in Statistics

Terms and Definitions in Statistics, Population and Sample, Raw Data, Types of variables,
Numerical variable (Continuous and discrete), Categorical variables (Nominal and ordinal),
Outcome and exposure variables, Display of data for 1 variable, for categorical data: Bar Chart
and Pie Chart, for numerical data: Histogram (different shapes) and Frequency Polygon
Measurements of central tendency: Mean, Median, quartiles, percentiles, Mode

Measures of spread: Range, Variance and Standard Deviation and its interpretation
Normal deviation and its characteristics
Unit 4: Probability, Permutations and combinations

Probability: Definition and basic formula, Probability of an event not occurring, Multiplicative
rule to calculate the probability of occurrence of both of two events. Independent events, Non-
independent events (conditional probability), Additive rule to calculate the probability of
occurrence of at least on of two events, mutually exclusive events, Non-exclusive events,
Concept of odds, Applications of probability in biology
Permutations: Definition and basic formula (nPr = n!/(n-r)!), Permutations with repetition,
Application of permutations in biology (The genetic code), Combinations: Definition and basic
formula (nCr = n!/r!(n-r)!), Application in biology (pedigree analysis), Problems involving
Permutations, Combinations and Probability

References:
1. Fundamentals of Biostatistics , 2006 – Bernard A Rosner
2. Fundamentals of Biostatistics, Khan and Khanum
3. Methods in Biostatistics, 2010, B.K. Mahajan
4. Fundamentals of Biostatistics, 2009 , V.B. Rastogi
5. Research Methodology: Methods and Techniques, 2004, C. R. Kothari
Practical Paper: Clinical Biochemistry, Molecular Biology, Enzymology

No. of Credits: 5
Session: 3 hours
I. Course Outcome
CO2: To isolate DNA and to study its properties
CO3: To differentiate between regulatory enzymes and non regulatory enzymes through kinetic
studies
Note:
experiment.
Clinical Experiments
1. Estimation of blood glucose by Arsenomolybdate.

2. Estimation of blood urea.
3. Estimation of serum uric acid.
4. Estimation of serum creatinine.

5. Estimation of glucosamine
6. Estimation of serum phosphorus
Enzyme practicals
7. Assay of salivary amylase.
8. Effect of pH on enzyme activity
9. Effect of enzyme concentration on enzyme activity
10. Effect of substrate concentration on enzyme activity
11. Effect of a competitive inhibitor on enzyme activity
12. Extraction and partial purification of an enzyme (amylase/peroxidase)
Liver Function Tests
13. Assay of serum transaminases – SGOT

14. Assay of Serum transaminases - SGPT.
15. Estimation of Alkaline Phosphatase
Molecular biology practicals
16. Verification of Chargaff’s rule by paper/ thin layer chromatography

17. Ultraviolet absorption spectrum of DNA and RNA
18. Determination of DNA concentration by UV absorption method
19. Determination of melting temperature and GC content
Fermentation Experiments
20. Estimation and recovery of citric acid.
References
2. Plummer: An introduction to Practical Biochemistry, 1988, Tata Mc Graw- Hill
education
5. Varley H: Practical Clinical Biochemistry, 1980, Heinemann, London
6. Thimmaiah S R: Standard Methods of Biochemical Analysis, 1999, Klayani Publishers
Semester VI
CORE Paper: Metabolism-II
No. of Credits: 04

I. Course Outcome
CO1: To compare breakdown and synthesis of fatty acids and its regulation,
CO2: To link the various pathways and cycles that contribute to synthesis of ATP, which in turn
would be used up for various synthetic pathways, thereby establishing ATP cycle.
CO3: To compare the roles of mitochondria and chloroplast in ATP synthesis.
CO4: To relate metabolism in different conditions, in different tissues, and how intermediates
connect several metabolic pathways, thus, relating a single pathway to various metabolic
disorders
a) Give a basic understanding of clinical aspects of biochemistry
c) Basic technical knowledge required in pathological laboratories
d) Work in industries related to diagnostics
e) Carry out basic research in understanding aspects of metabolism that are still not clear
II. Course Content
Unit 1: Metabolism of Lipids

Introduction, Lipoprotein metabolism, mobilization of fat, β-Oxidation of saturated, unsaturated
and odd chain fatty acids, energetic and regulation, alpha and omega oxidation, Ketone bodies
synthesis and utilization, FA synthesis, steps, stoichiometry, regulation, Desaturation and
elongation of FA, comparison of synthesis and oxidation
Biosynthesis of membrane lipids: TG & PL synthesis, Sphingolipids and glycolipids synthesis,

lipid storage diseases, role of liver and adipose tissue in lipid metabolism.
Unit 2: Energy Metabolism linked to Electron Transport System

PDH Complex, TCA Cycle, Energetics, Regulation, Anapleurotic & Amphibolic reactions,
Glyoxalate Cycle
Mitochondria, Glycerol Phosphate And Malate- Aspartate Shuttle, ETC, various hypotheses for
ATP Production, Oxidative Phosphorylation, Binding Change Hypothesis, P/O Ratio, Regulation
of oxidative phosphorylation, Uncouplers & Inhibitors, mitochondrially mediated diseases.

Unit 3: Photosynthesis
Structure of Chloroplast, light absorption, photosynthetic pigments, light harvesting systems of
plants and microbes, molecular architecture of Photosystem I and Photosystem II, Z-scheme of
photosynthetic electron flow, General features of photophosphorylation, Photo inhibition.
Evolution of oxygenic photosynthesis. Calvin-Benson cycle, regulation of Calvin cycle,
photorespiration, C4 and CAM pathways.
Unit 4: Integration of metabolism

Integration of metabolic pathways (carbohydrate, lipid and amino acid metabolic pathways),
Role of Hormones (Glucagon, Epinephrine, Insulin) in Fuel Metabolism, tissue specific
metabolism (brain, muscle, and liver), Metabolic adaptations in well-fed state, early fasting state,
fasting state, early re-fed state, energy requirements, reserves and caloric homeostasis, Metabolic
homeostasis during exercise, cardio vascular response.
1. Berg JM, and Tymoczko TJ Stryer L,: Biochemistry (7thed), (2012).WH Freeman
Publishers
2. Bhagvan NV: Medical Biochemistry (4thed) Bartlett Publishers.
3. Donald Voet and Voet J: Biochemistry (4thed) 2011, Wiley Publications.
4. Grisham and Garett: Biochemistry (5thed), (2013) Pearson-Thomson publishers
5. JeoffreyZubay: Principles of Biochemistry, McGraw Hill Publications, (1996).
6. Murray RK, Rodwell VW: Harpers review of Biochemistry (25thed), (2000).
7. Nelson DL and Cox MM: Lehninger’s Principles of Biochemistry (6thed) 2008.
8. Metzler D E: Biochemistry (2nded) (2003), Elsevier
9. Dee Unglaub Silverthron: Human Physiology an integrated approach (5thed), Pearson –
Benjamin Cummings (2010).
Semester VI
CORE Paper: Molecular Biology-II

No. of Credits: 04
I. Course Outcome
The main objective of the course will be to understand the concepts of molecular biology and its
techniques.
CO1: To explain complex mechanisms like homologous recombination and transposition and
look at the importance of these in the cells.
CO2: To appraise the basic tools required in recombinant DNA technology
CO3: To demonstrate the various techniques in molecular biology and their applications
CO4: To evaluate the use of recombinant DNA technology in betterment of the society
CO5: Appreciate experiments carried out by scientists to enable understand various molecular
mechanisms
a) To chose a career in molecular biology and genetic engineering
b) Exploit the basic understanding of the subject to create something that can help society
c) Equip oneself with skills to grow in the biotech sector
d) Work in biotechnology industries in Research and Development/Production/ Quality
Assurance
e) Carry out basic research in understanding many more molecular mechanisms inside a cell.
II. Course Content
Unit 1: Basic techniques of Molecular Biology

Separation of DNA and RNA molecules according to size using electrophoresis and
centrifugation; Purification of genomic DNA from various sources: Bacteria, plant cells and
animal cells; Quantification and assessment of purity of DNA using UV spectrophotometer;
Purification of plasmid; Purification of phage DNA: Lambda and M13.
Unit 2: Homologous Recombination and Transposition
Introduction to homologous recombination, Models for Homologous Recombination: The

Holliday Model, The Double – Strand Break Repair Model; Homologous Recombination protein
machines; Site specific recombination
Introduction to Transposition; Classes of Transposable elements (DNA Transposons,
Retrotransposons) and their mechanisms (Cut and Paste Mechanism, Copy and Paste
Mechanism); Maize elements in Barbara McLintoc’s studies.

Unit 3: Basic tools used in recombinant DNA Technology
Basic concepts of gene cloning; The range of manipulative enzymes; Cutting and ligation of
DNA; Introduction to Vectors; Types of Vectors (M13, lambda phage, pBR322 and pUC 8), and
its use in cloning; Host organisms used in cloning; Introduction of vectors into host organisms by
transformation using physical and chemical methods; Different methods of horizontal gene
transfer: Transformation, Conjugation and Transduction.
Unit 4: Specialized Techniques used in Molecular Biology

Construction of genomic library and cDNA library; Identification of clones in DNA library using
the concept of hybridization; Chemical synthesis of oligonucleotides; Polymerase Chain
Reaction and its types; Blotting Techniques: Southern, Northern, and Western; DNA Sequencing
methods: DNA sequencing: Sanger’s method of chain termination and Maxam Gilbert’s method
of chemical degradation; DNA Fingerprinting and its application.
1. Berg JM, and Tymoczko TJ, Stryer L,: Biochemistry (6th Edition)
2. Watson, J.D - Molecular Biology of the Gene (5th Edition)
3. De Robertis and De Robertis: Cell and Molecular Biology (8th Edition)
4. Donald Voet and Voet J: Biochemistry (4th Edition) 2011
5. Grisham and Garett: Biochemistry (3rd ed)
6. Benjamin Lewin: Genes IX (2007)
7. Nelson DL and Cox MM: Lehninger’s Principles of Biochemistry (5th ed) 2008
9. TA Brown. Gene Cloning and DNA Analysis (6th Edition), Wiley- Blackwell
Semester VI
CORE Paper: Immunology
No. of Credits: 04

I. Course Overview
The main objective of the course will be to understand the concepts of Immunology and its
important applications.
CO1: To describe the immune system of our body, the different organs and cells that enable us to
fight viruses and pathogens,
CO2: To assess the significance of antigen and antibody interactions and use this specificity for
various applications;
CO3: To explain underlying mechanisms allowing the immune cells and molecules to kill the
pathogens just like an army defends ones country
CO4: To fathom what would happen if the mechanisms sensitize our body such that it proves
detrimental to our own system eg. Asthmatic attacks
CO5: To prove that a natural phenomenon can be used as a basis to producing vaccines, which
have been responsible for eradication of diseases like small pox and now polio
CO6: To demonstrate that experiments carried out by scientists to enable understand the
mechanisms underlying immune responses
a) Working towards developing vaccines against many diseases
b) Use immune molecules or cells for diagnosis and therapy especially for cancer
c) Work in laboratories specifically using immune techniques like Radioimmunoassay,
ELISA etc.
d) Carry out basic research in understanding still unexplored areas of immunology.
II. Course Content
Unit 1: Introduction, Innate, Acquired, organs and cells of Immune system

Introduction, organs of immune system (primary and secondary), cells of immune system (B,T,
Null cells, mononuclear cell, granulocytes, mast cells, dendritic cells). Innate immunity
(anatomic barriers, physiological barriers, endocytic and phagocytic barriers, barriers created by
the inflammatory response), Acquired immunity, connections between innate and adaptive
immunity, cell adhesion molecules, chemokines, leukocyte extravasation, localized and systemic
response, self-versus non – self. Complement components, classical and alternate pathways,
MAC and its regulation, consequences of complement activation, complement deficiencies.
Unit 2: Ag, Ab, Ag-Ab interaction and experiments, Hybridoma technology

Immunological properties of antigen, factors that influence immunogenicity, Haptens, B and T
cell epitopes, antigenicity, mitogens.

Structure and functions of antibody, antigenic determinants on Ig, Isotypes of Ig, Ig super family.
Ag-Ab interactions, affinity, avidity, precipitations reactions, agglutination reactions, RIA,
ELISA, Western Blotting, Immuno fluorescence, Hybridoma technology and its uses, engineered
mAbs.
Unit 3: MHC, Ag processing & presentation, T & B cell response, Complement system
Structure and functions of Class I and II MHC, role of APC, Ag processing (endocytic and
cytosolic pathways), Ag presentation
Activation, maturation and differentiation of T cell receptors, Humoral response, Activation,
maturation and differentiation of B cells
Unit 4: Immune response: Tolerance, hypersensitivity, cytokines and Vaccines

Regulation of immune responsiveness, tolerance, hypersensitivity reactions (Type I, II, III, IV),
Properties of cytokines, receptors of cytokines, role in inflammatory response, active and passive
immunization (whole organism vaccines, purified macromoleucles as vaccines, recombinant
antigen and vector as vaccines, synthetic peptide, anti-idiotype vaccines).
1. Kuby Immunology (2007) 6th ed., Kindt, T.L., Goldsby, R.A. and Osborne, B.A., W.H
Freeman and Company (New York), ISBN:13: 978-0-7167-8590-3 / ISBN: 10:0-7617-
8590-0.
2. Immunology: A Short Course (2009) 6th ed., Coico, R and Sunshine, G., John Wiley&
sons, Inc (New Jersey), ISBN: 978-0-470-08158-7.
3. Janeway’sImmunobiology (2012) 8th ed., Murphy, K., Mowat, A., and Weaver, C.T.,
Garland Science (London & New York), ISBN: 978-0-8153-4243-4.
4. Immunology: Jan Klein, Blackwell Scientific
5. Immunology: Ivan Roitt, (10thed), Blackwell Scientific Press, 2010.
Semester VI
CORE Paper: Genetics

No. of Credits: 04
I. Course Overview
The main objective of the course will be to understand the concepts of Genetics and role of genes
in developmental biology
CO1: Apply the principles of Mendelian inheritance and their extensions by analysing
inheritance patterns from crosses
CO2: Map genes in microorganisms and eukaryotes by 2- or 3-point test crosses
CO3: Describe the origins and genetic consequences of mutations and chromosomal
abnormalities
CO4: Describe the concept of maternal inheritance, epigenetics and evolutionary genetics
CO5: Analyse basic processes in population genetics, mutation, migration, natural selection and
genetic drift and describe how they affect the genetic diversity within a species
CO6: Appreciate experiments carried out by scientists to enable understand genetics
The knowledge from this course can help in the following:

a) Explore career options in cytogenetics and genetic counselling
b) Work in laboratories dealing with prenatal genetic diagnosis of disorders
c) Work in clinical embryology field
d) Carry out basic research in understanding still unexplored areas of genetics.
II. Course Content
Unit 1: Mendelian Genetics and deviations from Mendel’s laws

Introduction to genetics; Mendelian Genetics: History of Mendelian genetics, First Law of
Inheritance, Second Law of Inheritance, Test Cross and Back cross and their significance.
Deviations: Incomplete Dominance, codominance, overdominance; Multiple alleles: ABO blood
group and incompatibility, Rh incompatibility; Epistasis: Dominant and Recessive epistasis with
examples; Non epistatic inter allelic gene interactions; Gene Lethality
Unit 2: Chromosomal basis of genetics

Chromosomal theory of inheritance and inheritance patterns; Sex linkage, non-disjunction as
proof of chromosomal theory of inheritance; Chromosomes: Chemical composition and
structural organization of chromatids; Centromeres and Telomeres; Chromatin and nucleosome
organization: eu- and heterochromatin; Special banding patterns in human chromosomes;
Chromosomal aberrations: structural and numerical; Evolution of wheat, cotton and rice;
Linkage and crossing over; Gene mapping; Interference and coincidence in prokaryotes and
eukaryotes; Isolation of auxotrophs and replica plating; Induced mutations in microbes, plants
and animals and its economic benefits; Analysis of mutations in biochemical pathways: one gene
– one enzyme hypothesis
Unit 3: Population genetics and Extrachromosomal Inheritance

Extrachromosomal inheritance; Mitochondrial equilibrium and evolution; Evolution of
chloroplast DNA and its inheritance; Examples of maternal inheritance
Population genetics: Hardy Weinberg theory, Factors affecting Hardy Weinberg theory, Gene
and genotypic frequencies; Pedigree analysis; Introduction to the concept of Epigenetics;
Evolutionary genetics
Unit 4: Principles of development

Introduction to development biology: Anatomical approaches to understand development of an
organism like comparative embryology, evolutionary embryology, medical embryology, and
mathematical models of developmental biology.
Life cycles and development patterns: The Evolution of Developmental Patterns in Unicellular
protists. Multicellularity: The Evolution of Differentiation, Developmental Patterns among the
metazoan.
Genes and development: The Embryological Origins of the Gene Theory, Evidence for Genomic
Equivalence, Differential Gene Expression, Determining the Function of Genes during
Development, Identifying the Genes for Human Developmental Anomalies.
III. Recommended learning Resources

1. Genetics (2012) 6th ed., Snustad, D.P. and Simmons, M.J., John Wiley &
Sons.(Singapore)
2. Genetics - A Conceptual Approach (2012), 4th ed., Pierce, B.A., W.H. Freeman & Co.
(New York)
3. An Introduction to Genetic Analysis (2010), 10th ed., Griffiths, A.J.F, Wessler, S. R,
Carroll, S. B. and Doebley, J., W.H. Freeman & Company (New York)
Semester VI
Subject Elective Paper: Model Organisms
No. of Credits: 02
I. Course Outcome
The main objective of the course will be to understand the importance of having a model
organism to study the basic metabolic and molecular pathways, to understand responses of
systems to external stimuli or environment, to enable research oriented towards understanding
basics as well as looking at applications etc. The features and characteristics that are needed to
make use of an organism for various studies are of prime importance. In future, many more such
model organisms could be developed to unravel the mysteries of life.
CO1: To highlight basic characteristics required in a model organism.

CO2: To design experiments using these model organisms.
CO3: To explain the concepts that have become clear because of research carried out using these
model organisms
a) Defining a problem and explore using model organisms to seek for a solution, thus
looking at research as a career option
b) Enable use of these model organisms to develop products for the market, by beginning a
start up company.
II. Course Content
Unit 1: Bacteriophage and E.coli

Bacteriophages: Basic features, types and its life cycle, Assays of phage growth, Phage Crosses
and Complementation Tests, Use as vectors; Advantages and disadvantages.
Bacteria: Basic features, growth and basic requirements, E. coli: the most commonly used
bacteria, Whole genome sequencing and transcriptional profiling, cytological analysis,
biochemical analysis studies, BACs; Advantages and disadvantages.
Unit 2: Yeast and Arabidopsis thaliana

Yeast: unicellular eukaryote, basic features, variations in size and multiplication, small
characterized genome, use in rDNA technology, plasmids and YACs, its feasibility for studying
mutations; Advantages and disadvantages.
Arabidopsis thaliana: Basic characteristics and growth pattern; Attributes of Arabidopsis as a
model genetic system; DNA transformation studies; developmental analysis by using fluorescent
markers; Advantages and disadvantages
Unit 3: C. elegans and Drosophila

C. elegans: Basic characteristics and rapid life cycle, well studied lineages, Drug toxicity studies
and cognitive functions; Discovery of cell death pathway and RNAi; Advantages and
disadvantages.
Drosophila: Basic characteristics and rapid life cycle, first genome maps, genetic mosaics, ease
of creating mutants, ease of creating transgenic fruitflies; Advantages and disadvantages.
Unit 4: Mus musculus and zebrafish

Mus musculus: Life cycle and basic characteristics; embryonic development dependence on stem
cells; creating transgenic mice; knockout mice; homologous recombination studies; epigenetic
inheritance; Advantages and disadvantages.
Zebrafish: Life cycle and basic features; developmental studies due to its regenerative properties;
mutations in genes; study of human diseases especially tuberculosis; Imaging studies using
fluorescence; Advantages and disadvantages.

III. Recommended learning Resources
1. Genetics (2012) 6th ed., Sinustad, D.P. and Simmons, M.J., John Wiley &
Sons.(Singapore)
2. Genetics - A Conceptual Approach (2012), 4th ed., Pierce, B.A., W.H. Freeman & Co.
(New York)
3. An Introduction to Genetic Analysis (2010), 10th ed., Griffiths, A.J.F, Wessler, S. R,
Carroll, S. B. and Doebley, J., W.H. Freeman & Company (New York)
4. Watson, J.D - Molecular Biology of the Gene (5th Ed)
6. Emerging model Organisms, Vol 1 and 2., CHL Press, 2010
Semester VI
Practical Paper: Biochemistry, Molecular Biology, Immunology and Genetics
No. of Credits: 5
Session: 3 hours
I. Course Outcome
CO1: To relate metabolism in different conditions, in different tissues, and how intermediates
connect several metabolic pathways, thus, relating a single pathway to various metabolic
disorders
CO3: Appreciate experiments carried out by scientists to enable understand various molecular
mechanisms
CO4: To demonstrate that experiments carried out by scientists to enable understand the
mechanisms underlying immune responses
CO5: Analyse basic processes in population genetics, mutation, migration, natural selection and
genetic drift and describe how they affect the genetic diversity within a species
CO6: Appreciate experiments carried out by scientists to enable understand genetics
Note:
experiment.

Biochemistry Experiments
1. Estimation of A/G ratio and its significance

2. Protein estimation by Bradford Assay
3. Estimation of Bilirubin
4. Estimation of Serum iron
5. Estimation of serum magnesium
6. Lipid Profile analysis (Case studies)
7. Isolation of cholesterol from egg yolk and its estimation.
8. Isolation of lecithin, identification by TLC, and its estimation.
9. Isolation of chloroplasts from spinach
10. Estimation of chlorophyll
11. Estimation of photosynthetic activity.
12. Estimation of nitrate reductase
Molecular biology practicals

13. Diauxic growth curve effect (Regulation of gene expression)
14. Isolation of DNA from WBCs and comment on purity
15. Effect of inhibitors on protein synthesis
Immunological Tests
16. Ouchterlony Double Radial Immunodiffusion

17. Mancini Single Radial Immunodiffusion.
18. Demonstration of Enzyme linked immunosorbent assay
19. Antibody structure and binding: computer based study
Genetics practicals
20. Study of abnormal human karyotype (Dry Lab)

21. Pedigree analysis (Dry Lab)
22. Population genetics studies (Case study: Blood groups in population)
23. e – PCR: computational study
References
2. Plummer: An introduction to Practical Biochemistry
5. Varley H: Practical Clinical Biochemistry

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St.

Xavier’s College (Autonomous), Ahmedabad-9

PO1. Create a strong knowledge domain/ expertise

PO2. Develop critical thinking, Problem solving and research aptitude

PO3. Skill development

PO5. Self-directed and lifelong learning

PO6. Developing employability and entrepreneurial skills

PO7. Promoting Ecological sustainability development

PO8. Nurturing creativity and humane values

Programme Specific Outcome for BSc Biochemistry

PSO4. Ability to communicate the understanding of the learning to others

CORE Paper: Fundamentals of Biochemistry

II. Course Content

Unit 1: Chemistry of life: An introduction

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 2

Measurement of pH: indicators, pH meter, different types of electrodes, advantages and

Chemical bonding (covalent, ionic, Hydrogen, Van der Waal’s, hydrophobic).

Configuration in sugars, reference carbohydrate, Fischer’s projection formula and representation

Oligosaccharides – Occurrence, structure, chemical name, function and importance of maltose,

Polysaccharides – Occurrence, structure, chemical name, functions and importance of starch,

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 3

Glycobiology: Glycosaminoglycans - Occurrence, structures and functions of hyaluronic acid,

Unit 3: Amino acids and Proteins

Complex lipids and Sterols: Glycerophospholipids – classification, properties and functions of

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 4

Structure and properties of sterols; Colour reactions of cholesterol.

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 5

Emphasis will be given to systematic designing of experiments in the laboratory sessions.

IV. Recommended Learning Resources

1. Biochemistry, 5th Edition. Garrett and Grisham

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 6

The course will give a detailed description of

By the end of the paper, a student should be able to

CO 2: To describe the importance of semi permeable nature of plasma membrane in maintaining

CO 3: To establish the concept of how proper conformations of lipids and proteins in a

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 7

CO 7: Appreciate experiments carried out by scientists to enable understand the working of a

a) Research in elucidation of molecular mechanisms within a cell

b) Research in cancer biology, tissue engineering, stem cells etc.

c) Drug discovery targeting various anomalies due to malfunction of organelles

II. Course Content

Unit 1: Nucleic acids and Origin of Life

Porphyrins: Introduction, nucleus, classifications, metalloporphyrins.

Unit 2: Structural components of cell

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 8

Unit 4: Cell cycle and Cell Senescence

Practical Paper: Fundamentals of Biochemistry

Experiments involving titrations

1. Estimation of amino acid by formal titration

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 9

Experiments based on lipids.

Experiments involving Qualitative Analysis

Experiments involving Colorimetric Estimations

18. Permanent slides of

B.Sc. Biochemistry Syllabus, St. Xavier’s College (Autonomous), Ahmedabad-9 Page 10

IV. Recommended learning Resources

1. Molecular Cell Biology, 7th Edition. Lodish, et. al.

By the end of the paper, a student should be able to:

CO 2: To differentiate between eubacteria, archaebacteria, fungi, algae and viruses and

CO 3: To justify the discovery and advancement of microscopic techniques has led to