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:
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:
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.
Discussion & Comments