Biomolecules
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14.27 How are vitamins classified? Name the vitamin responsible for the coagulation of blood.
14.27 How are vitamins classified? Name the vitamin responsible for the coagulation of blood.
14.27
Vitamins can be defined as the essential dietary factors required by an organism in minute quantities and whose absence causes specific deficiency Vitamins are broadly classified into two types:-
(i) Fat-soluble vitamins:
These are oily substances not readily soluble in water. These includ
14.26 What is the effect of denaturation on the structure of proteins?
14.26 What is the effect of denaturation on the structure of proteins?
14.26
During denaturation, 2-degree and 3-degree structures of proteins are destroyed but 1- degree structure remains intact. As a result of denaturation, The globular proteins (soluble in water) are converted into Fibrous proteins (insoluble in water) and their biological activity is lost. Fo
14.25
Enzymes are naturally occurring simple conjugate proteins acting as specific catalysts in all processes. In contrast to ordinary chemical catalyst, it loses activity by pH or temperature change.
For example:- the enzyme used to catalyze the hydrolysis of maltose into glucose is named as maltase.
14.24 How do you explain the amphoteric behaviour of amino acids?
14.24 How do you explain the amphoteric behaviour of amino acids?
14.24
Amino acids contain an acidic (carboxyl group) and a basic (amino) group within the same molecule. In aqueous solution, they neutralize each other. The carboxyl group loses a proton while the amino group accepts it. S a result, a dipolar or zwitter-ion is formed.

In zwitter ionic form, the
14.23 Differentiate between globular and fibrous proteins.
14.23 Differentiate between globular and fibrous proteins.
14.23
Globular proteins | Fibrous proteins |
It is usually soluble in water. | It is insoluble in water. |
All enzymes are globular protein. Some hormones such as insulin are also globular protein. | Fibrous proteins are usually used for structural purposes. For example, keratin is present in nails and hair; collagen in tendons; and myosin in muscles. |
The polypeptide chain in this protein is folded around itself, giving rise to spherical structure. | It is a fibre-like-structure formed by the polypeptide chain. These proteins are held together by strong and disulphide bonds. |
They are soluble in acids and bases. | They are insoluble in acids and bases. |
Examples:- egg albumin, casein of milk. | Examples :- Silk, Skin, Wool. |
They have weak intermolecular hydrogen bonding. | They have comparatively stronger intermolecular forces of attraction. |
They have folded, ball like structure. | They have thread like structure. |
Globular proteins are also called as spheroproteins owing to their shape. | Fibrous proteins are also called as scleroproteins. |
More sensitive to the changes in pH, temperature etc. | Less sensitive to the changes in pH, temperature etc. |
14.22 What type of bonding helps in stabilising the α-helix structure of proteins?
14.22 What type of bonding helps in stabilising the α-helix structure of proteins?
14.22
The stability of α-helix structure is due to intramolecular hydrogen bonding between –NH and –CO groups of polypeptide chain. The α-helix is known as 3.613 because each turn of α-helix contains approximately 3.6 amino acids and a 13-membered ring is formed by hydrogen bonding.
14.21 What are the common types of secondary structure of proteins?
14.21 What are the common types of secondary structure of proteins?
14.21
There are two common types of secondary structure of proteins:
(i) α–helix structure
(ii) β–pleated sheet structure
α–Helix structure
If the size of R-groups is quite large then the intramolecular bonds are formed between the C=O of one amino acid and the N-H group of the forth amino acid residue i
14.20 Define the following as related to proteins (i) Peptide linkage (ii) Primary structure (iii) Denaturation.
14.20 Define the following as related to proteins (i) Peptide linkage (ii) Primary structure (iii) Denaturation.
14.20
When two molecule of –amino acids similar or different combine in this way that the amino group of one molecule with carboxy group of the other molecule, this result in the elimination of water molecule and the formation of new bond-CO NH- .
This type of bond is called peptide bond or pept
14.19 What are essential and non-essential amino acids? Give two examples of each type.
14.19 What are essential and non-essential amino acids? Give two examples of each type.
14.19
(i) The amino acids which cannot be synthesised is called as essential amino acids. It must be obtained through diet. Example:- valine and leucine.
(ii) The amino acids which cannot be synthesised in the body is called as non-essential amino acids. Example: - glycine, Alanine.
14.18 Enumerate the reactions of D-glucose which cannot be explained by its open chain structure.
14.18 Enumerate the reactions of D-glucose which cannot be explained by its open chain structure.
14.18
Open structure of D-glucose could not explain the following reactions:
(i) Despite having the aldehyde group, glucose does not give 2,4 DNP test and Schiff's
(ii) Glucose does not react with sodium hydrogen sulphite to form addition
(iii) The absence of free –CHO group is shown when the penta-a