14.

BIOMOLECULES
 Carbohydrates: Polyhydroxy aldehydes or polyhydroxy ketones or compounds on
hydrolysis give carbohydrates.
 Classification of carbohydrates:
Monosaccharides
(a) Simplest carbohydrates
(b) It cannot be hydrolysed into simpler compounds
(c) Examples – Glucose, mannose
Oligosaccharides
(a) Carbohydrates which gives 2 to 10 monosaccharide units on hydrolysis
(b) Examples – Sucrose, Lactose, Maltose
Polysaccharides
(a) Carbohydrates which on hydrolysis give large number of monosaccharide units.
(b) Examples – Cellulose, starch
 Anomers: Pair of optical isomers which differ in configuration only around C1 atom
are called anomers. Examples – -D-glucopyranose and -D-glucopyranose.
 Epimers: Pair of optical isomers which differ in configuration around any other C
atom other than C1 atom are called epimers. E.g. D-glucose and D- mannose are
C2epimers.

Preparation of glucose (also called dextrose, grape sugar):

 From starch

 Structure of glucose

 Structure elucidation of glucose:

a) D – glucose with HI

b) D – glucose with HCN

c) D – glucose with NH2OH

d) D- glucose with Fehling’s reagent

e) D – glucose with Tollen’s reagent

f) D – glucose with nitric acid

g) D – glucose with (CH3CO)2O and ZnCl2

h) D – glucose with bromine water

i) Glucose with phenylhydrazine to form osazone

Glucose and fructose gives the same osazone because the reaction takes place at C1 and C2
only.

 Other Reactions of Glucose (Presence of ring structure)

Glucose does not give Schiff’s test and does not react with sodium bisulphite and NH3.
Pentaacetyl glucose does not react with hydroxyl amine. This shows the absence of –CHO
group and hence the presence of ring structure.

 Cyclic structure of glucose:

 Haworth representation of glucose:

 Cyclic structure of fructose:

 Haworth representation of fructose

  Glycosidic linkage: The oxide linkage formed by the loss of a water molecule when
two monosaccharides are joined together through oxygen atom is called glycosidic
linkage.

 Sucrose (invert sugar):

a) Sucrose is a non-reducing sugar because the two monosaccharide units are held together
by a glycosidic linkage between C1 of -glucose and C2 of – fructose. Since the
reducing groups of glucose and fructose are involved in glycosidic bond formation, sucrose is
a non-reducing sugar.

b) Sucrose is dextrorotatory but on hydrolysis it gives dextrorotatory & laevorotatory and the
mixture is laevorotatory.

 Haworth Projection of Sucrose:

 Maltose:

1. Maltose is composed of two α-D-glucose units in which C1 of one glucose (I) is

linked to C4 of another glucose unit (II).
2. The free aldehyde group can be produced at C1 of second glucose in solution and it
shows reducing properties so it is a reducing sugar.

 Haworth projection of maltose:

 Lactose (Milk sugar):It is composed of β-D-galactose and β-D-glucose. The linkage

is between C1 of galactose and C4 of glucose. Hence it is also a reducing sugar.

 Haworth projection of lactose:

 Starch: It is a polymer of -glucose and consists of two components — Amylose and

Amylopectin.

 Amylose:
 1. It is a water soluble component
2. It is a long unbranched chain polymer
3. It contains 200 – 1000 -D-(+)- glucose units held by – glycosidic
linkages involving C1 – C4glycosidic linkage
4. It constitutes about 15-20% of starch

 Amylopectin

1. It is a water insoluble component

2. It is branched chain polymer
3. It forms chain by C1 – C4glycosidic linkage whereas branching occurs by C1 –
C6glycosidic linkage
4. It constitutes about 80-85% of starch

 Cellulose:

1. It occurs exclusively in plants.

2. It is a straight chain polysaccharide composed only of -D-glucose units which are
joined by glycosidic linkage between C1 of one glucose unit and C4 of the next
glucose unit.

 Glycogen:

1. The carbohydrates are stored in animal body as glycogen.

2. It is also known as animal starch because its structure is similar to Amylopectin.
3. It is present in liver, muscles and brain.
4. When the body needs glucose, enzymes break the glycogen down to glucose.

 Amino acids:

Amino acids contain amino (–NH2) and carboxyl (–COOH) functional groups.

Where R – Any side chain

Most naturally occurring amino acids have L – Config.

 Types of amino acids:

a). Essential amino acids: The amino acids which cannot be synthesised in the body and
must be obtained through diet, are known as essential amino acids. Examples: Valine,
Leucine
b). Non-essential amino acids: The amino acids, which can be synthesised in the body, are
known as non-essential amino acids. Examples: Glycine, Alanine

 Zwitterion form of amino acids:

1. Amino acids behave like salts rather than simple amines or carboxylic acids. This
behaviour is due to the presence of both acidic (carboxyl group) and basic (amino
group) groups in the same molecule. In aqueous solution, the carboxyl group can lose
 a proton and amino group can accept a proton, giving rise to a dipolar ion known as
zwitter ion. This is neutral but contains both positive and negative charges.
2. In zwitterionic form, amino acids show amphoteric behaviour as they react both with
acids and bases.

 Isoelectric point: The pH at which the dipolar ion exists as neutral ion and does not
migrate to either electrode cathode or anode is called isoelectronic point.

 Proteins: Proteins are the polymers of -amino acids and they are connected to
each other by peptide bond or peptide linkage. A polypeptide with more than hundred
amino acid residues, having molecular mass higher than 10,000u is called a protein.

 Peptide linkage: Peptide linkage is an amide linkage formed by condensation

reaction between –COOH group of one amino acid and –NH2 group of another amino
acid.

Peptide link age

 Primary structure of proteins: The sequence of amino acids is said to be the

primary structure of a protein.

 Secondary structure of proteins: It refers to the shape in which long polypeptide

chain can exist. Two different types of structures:

– Helix:

1. It was given by Linus Pauling in 1951

2. It exists when R- group is large.
3. Right handed screw with the NH group of each amino acid residue H – bonded to – C
= O of adjacent turn of the helix.
4. Also known as 3.613 helix since each turn of the helix hasapproximately 3.6 amino
acids and a 13 – membered ring is formed by H – bonding.
5. C = O and N – H group of the peptide bonds are trans to each other.
6. Ramchandran angles ( and )– angle which makes with N – H
and angle which makes with C = O.

– pleated sheet:

1. It exists when R group is small.

2. In this conformation, all peptide chains are stretched out to nearly maximum
extension and then laid side by side which are held together by hydrogen bonds.
  Tertiary structure of proteins: It represents the overall folding of the polypeptide
chain i.e., further folding of the 2° structure.

 Types of bonding which stabilize the 3° structure:

1. Disulphide bridge (-S – S-)

2. H – bonding – (C = O … H – N)
3. Salt bridge (COO– … + )
4. Hydrophobic interactions
5. van der Waals forces

 Two shapes of proteins:

Fibrous proteins
a) When the polypeptide chains run parallel and are held together by hydrogen and disulphide
bonds, then fibre– like structure is formed.
b) These proteins are generally insoluble in water
c) Examples: keratin (present in hair, wool, silk) and myosin (present in muscles), etc
Globular proteins
a) This structure results when the chains of polypeptides coil around to give a spherical
shape.
b) These are usually soluble in water.
c) Examples: Insulin and albumins

 Quaternary structure of proteins:

1. Some of the proteins are composedof two or more polypeptide chains referred to as
sub-units.
2. The spatial arrangement of these subunits with respect to each other is known as
quaternary structure of proteins.

 Denaturation of proteins:

1. The loss of biological activity of proteins when a protein in its native form, is
subjected to physical change like change in temperature or chemical change like
change in pH. This is called denaturation of protein.
2. Example: coagulation of egg white on boiling, curdling of milk.

 Nucleoside:

1. Base + sugar

 Nucleotide:

1. Base + sugar + phosphate group

  Nucleic acids (or polynucletides):

1. Long chain polymers ofnucleotides.

2. Nucleotides are joined by phosphodiester linkage between 5’ and 3’ C atoms of a
pentose sugar.

 Two types of nucleic acids:DNA

1. It has a double stranded -helix structure in which two strands are coiled spirally
in opposite directions.
2. Sugar present is –D–2-deoxyribose
3. Bases:
i) Purine bases: Adenine (A) and Guanine (G)
ii) Pyrimidine bases: Thymine (T) and cytosine (C)
4. It occurs mainly in the nucleus of the cell.
5. It is responsible for transmission for heredity character.RNA

1. It has a single stranded -helix structure.

2. Sugar present is –D–ribose
3. Bases:
i) Purine bases: Adenine (A) and Guanine (G)
ii) Pyrimidine bases: Uracil (U) and cytosine (C)
4. It occurs mainly in the cytoplasm of the cell.
5. It helps in protein synthesis.

Double helix structure of DNA:

1. It is composed of two right handed helical polynucleotide chains coiled spirally in
opposite directions around the same central axis.
2. Two strands are anti-parallel i.e., their phosphodiester linkage runs in opposite
directions.
3. Bases are stacked inside the helix in planes to the helical axis.
4. Two strands are held together by H – bonds (A = T, G C).
5. The two strands are complementary to each other because the hydrogen bonds are
formed between specific pairs of bases.
6. Adenine forms hydrogen bonds with thymine whereas cytosine forms hydrogen bonds
with guanine.
7. Diameter of double helix is 2 nm.
8. Double helix repeats at intervals of 3.4 nm. (One complete turn)
9. Total amount of purine (A + G) = Total amount of pyramidine (C + T)

 Vitamins: Vitamins are organic compounds required in the diet in small amounts to
perform specific biological functions for normal maintenance of optimum growth and
health of the organism.
  Classification of vitamins: Vitamins are classified into two groups depending upon
their solubility in water or fat.

1. Water soluble vitamins i) These vitamins are soluble in water.

ii) Water soluble vitamins must be supplied regularly in diet because they are readily
excreted in urine and cannot be stored (except vitamin B12) in our body.
iii) Example: Vitamin C, B group vitamins.
2. Fat soluble vitamins
i) These vitamins are soluble in fat and oils but insoluble in water.
ii) They are stored in liver and adipose (fat storing) tissues.
iii) Example: Vitamin A, D, E and K

Important vitamins, their sources and their deficiency

diseases:
Name of
Sources Deficiency diseases
vitamins
xerophthalmia
Fish liver oil, carrots, butter
Vitamin A (hardening of cornea of eye)
and milk
Night blindness
Vitamin B1 Yeast, milk, green Beriberi
(Thiamine) vegetables and cereals (loss of appetite, retarded growth)
Cheilosis
Vitamin B2 Milk, egg white, liver, (fissuring at corners of mouth and lips),
(Riboflavin) kidney digestive disorders and burning sensation of
the skin.
Vitamin B6 Yeast, milk, egg yolk,
Convulsions
(Pyridoxine) cereals and grams
Pernicious anaemia
Vitamin B12 Meat, fish, egg and curd
(RBC deficient in haemoglobin)
Vitamin C Citrus fruits, amla and green Scurvy
(Ascorbic acid) leafy vegetables (bleeding gums)
Rickets
Exposure to sunlight, fish (bone deformities in children) and
Vitamin D
and egg yolk osteomalacia
(soft bones and joint pain in adults)
Vegetable oils like wheat Increased fragility of RBCs and
Vitamin E
germ oil, sunflower oil, etc. muscular weakness
Vitamin K Green leafy vegetables Increased blood clotting time

DNA and RNA Difference

DNA (Deoxyribonucleic acid) RNA (Ribonucleic acid)

 Definition

It is a long polymer. It has a deoxyribose and Is a polymer with a ribose and

phosphate backbone having four distinct phosphate backbone with four varying
bases: thymine, adenine, cytosine and bases: uracil, cytosine, adenine and
guanine. guanine.

Location

It is located in the nucleus of a cell and in the It is found in the cytoplasm, nucleus
mitochondria. and in the ribosome.

Sugar portion

It has 2-deoxyribose. It has Ribose.

Function

RNA is critical for the transmission of

The function of DNA is the transmission of
the genetic code that is necessary for
genetic information. It acts as a medium for
protein creation from the nucleus to
long-term storage.
the ribosome.

Predominant Structure

RNA is a single-stranded molecule

DNA is a double-stranded molecule that has
which has a shorter chain of
a long chain of nucleotides.
nucleotides.

Propagation

DNA replicates on its own, it is self- RNA does not replicate on its own. It is
replicating. synthesized from DNA when required.

Nitrogenous Bases and Pairing

The base pairing is as follows: GC (Guanine The base pairing is as follows: GC

pairs with Cytosine) A-T (Adenine pairs with (Guanine pairs with Cytosine) A-U
Thymine). (Adenine pairs with Uracil).
 Difference between Nucleotide and Nucleoside

Nucleotide Nucleoside

The chemical composition of

A nucleoside has a chemical
nucleotide consists of a phosphate
composition that consists of a sugar and
group, a sugar and a nitrogenous
a base without the phosphate group.
base.

They are one of the major causes of They are used as agents in medicine
cancer-causing agents to this very that are primarily used against viruses
day. and cancer-causing agents.

Some of the key examples of

Some of the major examples of
nucleosides are the same as nucleotides
nucleotides are adenosine, guanosine
only with the addition of phosphate
etc.
groups.
Following are the important difference between amylose and amylopectin:

Amylose Amylopectin

It is a straight- It is a branched-chain polymer of D-glucose

chain polymer of units
D-glucose units

Constitutes 20% Constitutes 80% of starch

of starch

It is soluble in It is insoluble in water

water

Straight chain Branched structure

structure

It contains α-1,4- It contains α-1,4-glycosidic bonds between two

glycosidic bonds glucose units in the straight chain and α-1,6-
between two glycosidic bonds at the branching
glucose units

Difference Between Essential and nonessential amino acids

Essential Amino Acids Nonessential Amino Acids

Definition

Essential amino acids are the amino Nonessential amino acids need not be
acids which have to be taken in taken in through diet as they can be
through diet as they “CAN NOT” be produced by the body
produced by the body

Number of Amino Acids

9 amino acids out of 20 are thought to 11 of the 20 amino acids are non-
be essential essential
 Sources

As the definition implies, essential Are produced within the body from
amino acids have to be acquired other amino acids and other
through food – such as soy, quinoa, components
egg, chicken, meat or vegetable
protein

Role

Serves to build and repair muscle Removal of toxins, integral in the

tissues. Also, it forms precursor synthesis of RBC and WBC, promotes
molecules for the formation of brain function and many more.
neurotransmitters in the brain

Deficiency

Highly probably as these amino acids Probability of deficiency is rare, but

are acquired through food can still occur due to starvation or
illness.

Difference Between Starch And Cellulose

Properties Starch Cellulose

Alpha/Beta 2 types of alpha glucose 1 type of beta glucose

Connection By alpha linkage By beta linkage

Digestion Easily digested Difficult to digest

Solubility Dissolves in warm water Does not dissolve in water

Strength Weaker than cellulose Strong

Crystalline Less crystalline More crystalline than starch

Consumption Can be consumed by humans Cannot be consumed by humans

Linkage Starch has alpha 1,4 linkage Cellulose has beta 1,4 linkage

Uses Plants use starch to store Plants use cellulose to support

energy structure

Reducing Sugar
 Reducing sugar is one that possesses a free aldehyde or ketonic group.
 It can reduce Fehling and Tollens reagent.
 Fehling A is Copper sulfate CuSO4and Fehling B is an aqueous solution of potassium
sodium tartrate KNaC4H4O6·4H2O.
 Tollens's reagent is the ammoniacal solution of silver nitrate ([Ag(NH3)2]+)
 Reducing sugar can act as a reducing agent.
 It can be further reduced to alcohol.
 For example maltose and lactose.

Non reducing sugar

 In a basic aqueous solution, a non-reducing sugar is not reduced by a weak oxidising
agent (one that oxidises aldehydes but not alcohols, such as Tollen's reagent).
 There is no free aldehyde or ketonic group.
 Non-reducing sugars do not have an -OH group attached to the anomeric carbon so
they cannot reduce other compounds.
 E.g. sucrose and Raffinose
 The structure of sucrose is as follows:-