Q.43 Collagen, α-keratin and tropomyosin have common structural features. They are P) disulfide bridges to neighboring proteins. Q) repeating sequences of amino acids R) a high β-sheet content S) superhelical coiling (A) P, Q (B) Q, R (C) Q, S (D) P, R

Q.43 Collagen, α-keratin and tropomyosin have common structural features. They are

P) disulfide bridges to neighboring proteins.

Q) repeating sequences of amino acids

R) a high β-sheet content

S) superhelical coiling

(A) P, Q

(B) Q, R

(C) Q, S

(D) P, R


Correct Answer

Option (C): Q and S


Explanation

Collagen, α-keratin, and tropomyosin are fibrous proteins, and they share specific structural principles that distinguish them from globular proteins.


Explanation of Each Statement

P) Disulfide bridges to neighboring proteins – ❌ Incorrect

  • Disulfide bonds are prominent in α-keratin, especially in hair and nails.

  • Collagen and tropomyosin do not primarily rely on inter-protein disulfide bridges.

  • Since this feature is not common to all three, this option is incorrect.


Q) Repeating sequences of amino acids – ✅ Correct

  • Collagen: Repeating Gly–X–Y sequence (often proline and hydroxyproline).

  • α-Keratin: Repetitive heptad sequences important for coiled-coil formation.

  • Tropomyosin: Repeating amino acid patterns stabilize its elongated structure.

  • ✔️ This feature is common to all three proteins.


R) A high β-sheet content – ❌ Incorrect

  • α-keratin is rich in α-helices, not β-sheets.

  • Collagen forms a triple helix, not β-sheet structures.

  • Tropomyosin is also predominantly α-helical.

  • Hence, this statement is false.


S) Superhelical coiling – ✅ Correct

  • Collagen: Three polypeptide chains form a right-handed triple helix.

  • α-Keratin: Two α-helices twist to form a coiled-coil (superhelix).

  • Tropomyosin: Exists as a coiled-coil dimer.

  • ✔️ Superhelical coiling is a shared structural feature.


Why Option (C) Is Correct

  • Both repeating amino acid sequences (Q) and superhelical coiling (S) are present in collagen, α-keratin, and tropomyosin.

  • Other options include features that are not common to all three proteins.

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