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NCERT · Class 12 · Chemistry

Chapter 10: Biomolecules

Practice each question, then open the answer or worked solution.

Textbook exercises

33 questions
Q21Written answer

What are the common types of secondary structures of proteins?
Proteins mainly have two common secondary structures—α-helix and β-pleated sheet.

  • α-helix: Right-handed helical structure stabilized by hydrogen bonds between nearby amino acids.
  • β-pleated sheet: Sheet-like arrangement stabilized by hydrogen bonds between parallel or antiparallel stretches of polypeptide chain.

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Q22Written answer

What type of bonding helps in stabilizing the α-helix structure of proteins?

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Answer: The α-helix structure in proteins is stabilized by hydrogen bonds between the -NH2 group of one amino acid and the -COOH group of another amino acid in nearby turns of the helix.

Q23Written answer

Differentiate between globular and fibrous proteins.

Fibrous protein Globular protein
It is a fibre-like structure formed by the polypeptide chain. They are held together by strong hydrogen and disulphide bond. The polypeptide chain in this protein is folded around itself, which gives rise to a spherical structure.
Insoluble in water. Soluble in water.
Used for structural purposes. For example, keratin is present in nails and hair; collagen is present in tendons, and myosin is present in muscles. All enzymes along with some hormones such as insulin are globular proteins.

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Q24Written answer

How do you explain the amphoteric behaviour of amino acids?
Amino acids act as both acids and bases due to carboxyl and amino groups, forming zwitterions.

  • The carboxyl group donates a proton, and the amino group accepts a proton when in water, creating a dipolar ion known as a zwitterion.
  • This property allows amino acids to react both as acids and as bases.

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Q25Written answer

What are enzymes?

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Answer: Enzymes are proteins that act as biological catalysts. They help speed up reactions inside living things, work on specific substrates, and their names usually end in '-ase' (e.g., maltase or oxidoreductase).

Q26Written answer

What is the effect of denaturation on the structure of proteins?
Denaturation disrupts the protein's structure except for the sequence of amino acids.

  • Denaturation causes the protein’s globular structure to unfold and its helix to uncoil, losing its function.
  • The primary structure (amino acid sequence) remains unchanged; only secondary and tertiary structures are lost.
  • An example is the hardening of egg white on boiling.

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Q27Written answer

How are vitamins classified? Name the vitamin responsible for the coagulation of blood.
 Vitamins are classified by their solubility; vitamin K is needed for blood clotting.

  • Vitamins are divided into fat-soluble (A, D, E, K) and water-soluble (B group, C) categories.
  • Vitamin K helps the blood coagulate (clot).

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Q28Written answer

Why are vitamin A and vitamin C essential to us? Give their important sources.

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Answer: Deficiency of vitamin A causes night blindness and eye problems; its sources include fish liver oil, carrots, butter, and milk. Lack of vitamin C leads to scurvy (bleeding gums); it is present in citrus fruits and green leafy vegetables.

Q29Written answer

What are nucleic acids? Mention their two important functions.
Nucleic acids are biomolecules in cell nuclei that store genetic information and help synthesize proteins.

  • Nucleic acids are found in the nuclei of living cells as components of chromosomes (main types: DNA and RNA).
  • Functions:
    • DNA controls inheritance of traits (heredity).
    • DNA and RNA are involved in protein synthesis within cells.

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Q30Written answer

What is the difference between a nucleoside and a nucleotide?
Both are made from sugar and base, but nucleotides also have phosphoric acid.

  • Nucleoside = sugar + base. Example: base joined to the 1’position of the sugar.
  • Nucleotide = sugar + base + phosphoric acid. All three parts are joined together.

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