Biomolecules - II

Proteins
 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.

 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.
 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 by grouping of them through H-bonding
 . Two different types of secondary structures :
α– 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 has approximately 3.6
amino acids and a 13 – membered ring is formed by H – bonding.
Β- 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 to give compact , 3D molecular shape of
protein
Types of bonding which stabilize the 3° structure:
1. Disulphide bridge (-S – S-)
2. H – bonding – (C = O … H – N)
3. 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) Not affected by change in temperature or pH of solution.
d) 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) Get affected by change in temperature or pH of solution
c) Examples: Insulin and albumins
Quaternary structure of proteins:
1. Some of the proteins are composed of 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: contain only two components of nucleic acid
i.e. Base + sugar
Nucleotide: contain all three components of nucleic acid
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 α-helix structure in which two strands are coiled spirally
in opposite directions.
2. Sugar present is β–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 β –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.
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