Biochemistry—Secondary Structure In the β-pleated sheet, which of the following statements best describes its key features?

Difficulty: Easy

Correct Answer: All of the above.

Explanation:


Introduction / Context:
β-Pleated sheets are one of the two principal protein secondary structures, stabilized by inter-strand hydrogen bonding. This question tests recognition of hydrogen-bonding patterns, strand orientation, and chain conformation in β-sheets.


Given Data / Assumptions:

  • β-Sheets comprise at least two β-strands.
  • Hydrogen bonds form between C=O and N-H groups of adjacent strands.
  • Strands can be parallel or antiparallel.
  • Each strand is extended (zig-zag), not tightly coiled.


Concept / Approach:
Identify the defining characteristics: inter-strand hydrogen bonds, orientation variability (parallel/antiparallel), and extended backbone geometry. If all listed statements are standard features, “All of the above” is correct.


Step-by-Step Solution:

Step 1: Hydrogen bonding. In β-sheets, backbone atoms from neighboring strands form hydrogen bonds; this is a hallmark feature.Step 2: Orientation. β-Strands can align parallel (same N→C) or antiparallel (opposite directions); both are widely observed.Step 3: Conformation. Each strand is extended; the sheet is “pleated” due to tetrahedral geometry, not coiled like an α-helix.


Verification / Alternative check:
Ramachandran plots show β-strand phi/psi angles consistent with extended conformations. Structural databases showcase both parallel and antiparallel sheets.


Why Other Options Are Wrong:

  • Options A–C are not wrong; they collectively describe β-sheets. Hence D is correct and E is incorrect.


Common Pitfalls:
Confusing intra-strand with inter-strand hydrogen bonds; assuming only antiparallel sheets exist; picturing sheets as flat without pleats (the pleating is subtle but real).


Final Answer:
All of the above.

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