The major reason that antiparallel $\beta$-stranded protein structures are more stable than parallel $\beta$-stranded structures is that the latter:
A) are in a slightly less extended configuration than antiparallel strands.
B) do not have as many disulfide crosslinks between adjacent strands.
C) do not stack in sheets as well as antiparallel strands.
D) have fewer lateral hydrogen bonds than antiparallel strands.
E) have weaker hydrogen bonds laterally between adjacent strands.

Question

Quizplus · Accepted Answer

Antiparallel β-strands form stronger hydrogen bonds because the strands are aligned in opposite directions, allowing for optimal hydrogen bond geometry between the amide and carbonyl groups of the peptide backbone. In parallel β-strands, the alignment is less optimal, leading to weaker hydrogen bonds.

The Major Reason That Antiparallel β\betaβ -Stranded Protein Structures Are More Stable Than Parallel

The Major Reason That Antiparallel $\beta$ -Stranded Protein Structures Are More Stable Than Parallel