Respuesta :
Answer:
(c) QKASVEMAVRNSG
Explanation:
The alpha helix is a protein arrangement tightly packed, thereby the peptide will form a rod. The option (c) is expected to form an alpha helix because it contains three amino acids charged which are aligned on the face of the helix, 1-two residues positively charged: Lysine (K) and Arginine (R), and 2-one residue negatively charged: Glutamic Acid (E).
The following polypeptides are most likely to form an α-helix explain your answer - (c) QKASVEMAVRNSG
Destabilization of α-helices
The formation of alpha-helix required correct steric configuration. Amino acids with R-groups are too large like tryptophan, and tyrosine or too small glycine destabilize α-helices.
Proline also destabilizes α-helices has irregular geometry and causes steric hindrance because its R-group bonds back to the nitrogen of the amide group.
Option(A) CRAGNRKIVLETY
There is Glycine in this sequence, so it can not form an alpha helix.
Option (B): SEDNFGAPKSILW
The presence of glycine and proline causes not to form an alpha helix.
Option (C): QKSVEMAVRNSG
Glycine is present but still, it is most likely to form an alpha helix as glycine is the end of the sequence.
Find more information about a-helices:
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