Explore topic-wise InterviewSolutions in .

• plants – starch.
• In animals – Glycogen.

1. There are two types of secondary structure of protein: a-helix and pleated sheets. 

2. The polypeptide chain is arranged in a spiral helix. These spiral helices are of two types: a-helix (right handed) and Phelix (left handed). 

3. This spiral configuration is held together by hydrogen bonds. 

4. The sequence of amino acids in the polypeptide chain determines the location of its bend or fold and the position of formation of hydrogen bonds between different portions of the chain or between different chains.

Thus, peptide chains form an a-helix structure. 

5. Example of a-helix structure is keratin. 

6. In some proteins two or more peptide chains are linked together by intermolecular hydrogen bonds. Such structures are called P-pleated sheets. 

7. Example of P-pleated sheet is silk fibres. 

8. Due to formation of hydrogen bonds peptide chains assume a secondary structure.

1. The induced fit model shows that enzymes are flexible structures in which the active site continually reshapes by its interactions with the substrate until the time the substrate is completely bound to it. It is also the point at which the final form and shape of the enzyme is determined. 

2. Three-Dimensional conformation: 

a. All enzymes have specific 3-dimensional conformation. 

b. They have one or more active sites to which substrate (reactant) combines. 

c. The points of active site where the substrate joins with the enzyme is called substrate binding site.

The correct answer is (D) sugar + N-base + phosphate

The correct answer is (C) structural

The linear sequence of amino acids in polypeptide chain of a protein forms the primary structure of a protein.

The type of bond shown in the diagram is hydrogen bond.

When the inhibitor closely resembles the substrate in its molecular structure and inhibits the activity of the enzyme, it is known as a competitive inhibitor and the process is called competitive inhibition. Due to its close structural similarity with the substrate, the inhibitor competes with the substrate for the substrate-binding site of the enzyme. Consequently, the substrate cannot bind and as a result, the enzyme action declines.

Eg:- Inhibition of succinic dehydrogenase by malonate which closely resembles the substrate succinate in structure.

Number of fatty acids in triglyceride is 3.

The amino acids exists as Zwitter ions H₃N⁺ -CHRCOO^- , due to this dipolar salt like character, they have dipole- dipole interactions. 

Therefore, their melting points are higher than corresponding haloacids which do not have salt like character.

Due to salt like character amino acids interact strongly with water. As a result their solubility in water is higher than corresponding haloacids which do not have salt like character. 

Option : (b) Uracil

Option : (b) polypeptides

Option : (c) amino acids

Non-reducing sugars : 

Carbohydrates which do not reduce Fehling solution and Tollen’s reagent are called non-reducing sugars. E.g. sucrose.

Reducing sugars : Maltose or lactose 

Non-reducing sugars : Sucrose.

Option : (a) glycine