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Chem XII Biomolecules (L-2) 1

 Biomolecules

Chem XII Biomolecules (L-2) 2

Session Objective:
 Structure of Proteins

 Nucleic acid

 DNA and RNA

Chem XII Biomolecules (L-2) 3

Proteins

Proteins are the most abundant biomolecules of the living

system. They are required for growth and maintenance of
body.

All proteins are polymers of a-amino acids.

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Amino Acids

The amino acids are the compounds containing at least one

amino (–NH2 )and o ne ca r
boxy
l(– CO OH) function algro up.

The amino acids are classified as , , ,  and so on

depending upon the position of the two functional groups in
the alkyl chain.

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Non-essential Amino Acids

There are 20 different amino acids, each with a different – R

group, commonly found in the proteins of living things.

The human body can synthesis 10 out of the 20 amino acids

found in the proteins. These are called non-essential amino
acids, e.g., glycine, alanine, aspartic acid, glutamic acid, etc.

Chem XII Biomolecules (L-2) 6

Essential Amino Acids

Certain amino acids are required for proper health and growth
in human beings. But the human body is unable to synthesis
them.

These must be supplied through foods and are called

essential amino acids, e.g., valine, leucine, phenylalanine,
tyrosine, etc.

Chem XII Biomolecules (L-2) 7

Peptide Linkage

Chemically, peptide linkage is an amide formed between

–COOH group and –NH group. The reaction between two
molecules of similar or different amino acids, proceeds
through the combination of the amino group of one molecule
with the carboxyl group of the other the elimination of a water
molecule and formation of a peptide bond –CO–NH–.

Chem XII Biomolecules (L-2) 8

Dipeptide

The reaction between two molecules of similar or different

amino acids, proceeds through the combination of the amino
group of one molecule with the carboxyl group of the other,
resulting into the elimination of a water molecule and
formation of a peptide bond, – CO – NH –.

The product of the reaction is called a dipeptide. If three

amino acids combine, the product is a tripeptide and so on.

Chem XII Biomolecules (L-2) 9

Protein

A polypeptide with more than hundred amino acids residues,

having molecular mass higher than 10,000u is called a protein.

Classification of Protein

1. Fibrous proteins.
2. Globular proteins.

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Fibrous Proteins

In fibrous proteins, the polypeptide chains run parallel and

are held together by hydrogen and disulphide bonds. They
are insoluble in water. For example, keratin (present in hair,
wool, silk) and myosin (present in muscles), etc.

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Globular Proteins

In globular proteins, the polypeptide chain is folded, looped

and twisted so that the molecules are more or less spherical.
They are soluble in water.

For example, egg albumin, hemoglobin, enzymes and some

hormones like insulin.

Chem XII Biomolecules (L-2) 12

Classification of Proteins on the basis of structure

Primary Structure of Protein

It is the unique sequence of amino acid in each kind of

protein. It is not affected by usual action of pH change, acids
and alkalies and electrolytes.
(i.e. no denaturation for primary structure of protein.

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Secondary Structure of Proteins

The polypeptide chain gets folded due to intra-molecular

hydrogen bonding between the carboxyl and amino group. In
an -helix, the peptide chain coils and the turns of coil are
held together by hydrogen bonds. In -pleated sheet structure,
the polypeptide chains are stretched out.

Chem XII Biomolecules (L-2) 14

Tertiary Structure of Proteins

It is the three dimensional structure of globular proteins. It

arises due to folding and superposition of various secondary
structural elements. The main forces which stabilise the 2°
and 3° structures of proteins are hydrogen bonds, disulphide
linkages, van der Waals and electrostatic forces of attraction.

Chem XII Biomolecules (L-2) 15

Quaternary Structure of Proteins

Some of the proteins are

composed of two or
more polypeptide chains
referred to as sub-units.
The spatial arrangement
of these sub-units with
respect to each other is
known as quaternary
structure.

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Zwitter Ion- Dipolar

In zwitter ionic form, amino acids show amphoteric behaviour as

they react both with acids and bases.
These are water-soluble, high melting solids and 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 neutral but contains
both positive and negative charges.

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Denaturation

Denaturation refers to the loss of a biological activity of a

protein brought about by changes in its secondary and tertiary
structure due to heat, pH change, presence of salts, etc.

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Enzymes

Enzymes are naturally occurring simple or conjugated

proteins that catalyse biological reactions.

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Vitamins

Vitamins are substances necessary to maintain normal health,

growth and nutrition. They cannot be made by organisms and
so have to be supplied in the diet. Vitamins A, D, E and K are
fat soluble whereas vitamins B and C are water soluble.

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Types Vitamins

Fat soluble – (ADEK) Fat soluble – (ADEK)

Water Soluble- (Vitamin – B & C) excluding vitamin B1

2

Name of Sources Deficiency

Vitamins diseases
Vitamin-A Fish liver oil, carrots, Xerophthalmia
butter and milk (hardening of cornea of
eye)

Vitamin-B1Yest, milk, green Beri beri (loss of

vegetables and cereals appetite, retarded
Milk, eggwhite, liver, growth)
kidney

Chem XII Biomolecules (L-2) 21

Types Vitamins

Name of Deficiency
Sources
Vitamins diseases

Vitamin-B2 Milm, eggwhite, liver, Cheilosis (fissuring at

(Riboflavin) kidney corners of mouth and lips)
, digestive disorders and
burning sensation of the
skin.

Vitamin-B6 Yeast, milk, egg yolk, Convulsions

(Pyridoxine) cereals and grams

Vitamin-B1
2 Meat, fish, egg and Pernicious anaemia (RBC
curd deficient in haemoglobin)

Chem XII Biomolecules (L-2) 22

Types Vitamins

Name of Deficiency
Sources
Vitamins diseases

Vitamin-C Citrus fruits, amla Scurvy (bleeding gums)

(Ascorbic acid) and green leafy
vegetables

Vitamin-D Sunlight, fish and Rickets, osteomalacia

egg yolk

Vitamin-E Vegetable oils like Increased fragility of

wheat germ oil, RBCs and muscular
sunflower oil, etc. weakness

Vitamin-K Green leafy Increased blood clotting

vegetables time

Chem XII Biomolecules (L-2) 23

Types of Nucleic Acid

(i) Nucleotide (ii) Nucleoside

A Nucleotide Consists of three parts:

A five carbon atom sugar units, which is either ribose and

deoxyribose.

A nitrogen containing heterocyclic base

A phosphate group.

Chem XII Biomolecules (L-2) 24

Types of Nucleic Acid

The nitrogen containing bases in nucleotides belong to the

following two classes:

Purines: The bases derived from purines are adenine (A)

and guanine (G).

Pyrimidines: The bases derived from pyrimidines are

cytosine (C), thymine (T) and uracil (U).

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Nucleoside = Nucleotide
– Phosphoric Acid group

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 DNA and RNA differ from each other in the following
aspects:

DNA RNA
DNA carries the RNA is responsible for
genetic information protein synthesis
The sugar in DNA is The sugar in RNA is
2-deoxyribose. ribose

DNA consists of RNA consists of

ATGC base pair AUGC base pair
DNA is double helically RNA is single stranded
coiled structure

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 Types of RNA

Messenger RNA (m-RNA)

Ribosomal RNA (r-RNA)

Transfer RNA (t-RNA)

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Mutation

A mutation is a chemical change in a DNA molecule that

could lead to synthesis of proteins with an altered amino acid
sequence.

The changes in a DNA molecule can happen spontaneously or

may be caused by radiation, chemical agents or viruses.

Chem XII Biomolecules (L-2) 29

Exercises
11. What are essential and non-essential amino acids? Give two
examples of each type.

12. Define the following as related to proteins

(i) Peptide linkage (ii) Primary structure
(iii) Denaturation.

13. Differentiate between globular and fibrous proteins.

14. How do you explain the amphoteric behaviour of amino acids?

15. What are enzymes?

16. What is the effect of denaturation on the structure of proteins?

Chem XII Biomolecules (L-2) 30

Exercises
17. What are enzymes?
18. What is the effect of denaturation on the structure of proteins?

19. How are vitamins classified? Name the vitamin responsible for
the coagulation of blood.
20. Why are vitamin A and vitamin C essential to us? Give their
important sources.
21. What are nucleic acids? Mention their two important functions.

22. What is the difference between a nucleoside and a nucleotide?

23. The two strands in DNA are not identical but are complementary.
Explain.

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Exercises
24. Write the important structural and functional differences
between DNA and RNA.

25. What are the different types of RNA found in the cell?

Chem XII Biomolecules (L-2) 32

 Thank You

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