This set of Class 12 Chemistry Chapter 14 Multiple Choice Questions & Answers (MCQs) focuses on “Biomolecules – Proteins – 2”.
1. Proteins are formed primarily from ______ bonds.
a) glycosidic
b) peptide
c) phosphodiester
d) disulphide
View Answer
Explanation: When many alpha amino acid units arranged themselves in a chain (or any other suitable structure), a protein is formed. These units are linked together by peptide bonds between NH2 groups and COOH groups.
2. Identify the correct statement.
a) Peptide bond is formed by the loss of water molecule
b) A protein is made of only one type of amino acid
c) Dipeptides consists of different amino acids
d) Glycylalanine is a tripeptide
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Explanation: The reaction between two molecules of same of different amino acids proceeds through the linking of COOH group of one and the NH2 group of the other along with the loss of H2O and formation of a peptide bond. The product is called a dipeptide.
3. How many peptide linkages does a hexapeptide have?
a) 4
b) 5
c) 6
d) 7
View Answer
Explanation: A hexapeptide is a compound formed by the combination of six same or different amino acids with the help of the amino and carboxyl groups. The six amino acids are connected by five peptide bonds.
4. Proteins are _______
a) dipeptides
b) tripeptides
c) tetrapeptides
d) polypeptides
View Answer
Explanation: When the number of amino acids in a peptide is more than ten, it is a polypeptide. But when a polypeptide has more than a 100 amino acid residues, with molecular mass higher than 10000u, it is called a protein. However, this is not true in all cases (like insulin).
5. Alanylglycyl phenylalanine is an example of a ______
a) dipeptide
b) tripeptide
c) tetrapeptide
d) polypeptide
View Answer
Explanation: It is a tripeptide made from alanine, glycine and phenylalanine. It is abbreviated as Ala-Gly-Phe. The carboxyl group of alanine and the amino group of glycine combine to form one peptide bond. The second peptide linkage is formed between COOH of glycine and NH2 of phenylalanine.
6. Which of the following bonds in not found in fibrous proteins?
a) Phosphodiester
b) Peptide
c) Hydrogen bonds
d) Disulphide
View Answer
Explanation: Fibrous proteins are linear polypeptide chains that lie parallel to each other. Peptide binds are prevalent in the individual chains, whereas the threads are held together by hydrogen and disulphide bonds, to form a fibre-like structure.
7. Which of the following is not a fibrous protein?
a) Keratin
b) Myosin
c) Collagen
d) Albumin
View Answer
Explanation: Keratin is a fibrous protein found in skin, nails, hair and wool. Myosin is present in muscles and collagen in tendons. Albumin is a globular protein.
8. The sequence in which amino acids are arranged in a protein is called ______ structure.
a) primary
b) secondary
c) fibrous
d) sheet
View Answer
Explanation: Proteins have one or more polypeptide chains, in which each chain consists of a specific sequence of amino acids linked with each other. This is called the primary structure and is the most basic level. Any change in primary structure creates a different protein.
9. Which type of bonds govern the secondary structure of proteins?
a) Covalent
b) Hydrogen
c) Electrostatic
d) Peptide
View Answer
Explanation: The secondary structure refers to the shape in which the polypeptide chain exists. There are two possible structures which arise due to the regular folding of the backbone of the polypeptide chain due to hydrogen bonding between CO and NH groups of peptide bond.
10. Which of the following is soluble in water?
a) Insulin
b) Elastin
c) Fibroin
d) Collagen
View Answer
Explanation: Fibroin (silk), collagen (tendons) and elastin (skin) are fibrous proteins which are insoluble in water. Insulin is an example of a globular protein which is water soluble.
11. The structure in which all peptide chains are stretched out to full extension and laid side by side through intermolecular hydrogen bonds is called ______
a) α-helix
b) β-pleated sheet
c) tertiary structure
d) quaternary structure
View Answer
Explanation: β-pleated sheet is one of the secondary structures of proteins formed due to intermolecular hydrogen bonding. The structure resembles the pleated folds of drapery and hence the name.
12. Fibrous and globular proteins are classified on the basis of ______ structure.
a) primary
b) secondary
c) tertiary
d) quaternary
View Answer
Explanation: Tertiary structure represents the overall folding of the polypeptide chains or the further folding of secondary structures. It gives rise to two major molecular shapes, i.e., fibrous and globular.
13. A protein ‘X’ was found in a biological system with a unique 3-D structure and biological activity. ‘X’ is known as _______
a) tertiary structure
b) quaternary structure
c) native protein
d) globular protein
View Answer
Explanation: Native state of a protein is its most energetically stable state. When a native protein is subjected to physical change, the hydrogen bonds are disturbed, and the globules unfold.
14. The primary structure of protein is unaffected by denaturation.
a) True
b) False
View Answer
Explanation: Denaturation is the process of altering the physical and biological properties of proteins without affecting chemical composition. It is caused by subjecting the protein to physical changes like temperature, pH, etc. During this, the secondary and tertiary structures are destroyed but the primary structure remains intact.
15. Boiling an egg is an example of reversible denaturation.
a) True
b) False
View Answer
Explanation: The egg white gets coagulated on boiling. The globular proteins in egg white (albumin) change to a rubber like insoluble mass. This is irreversible denaturation as the protein cannot return to its original state.
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