A new drug is developed which selectively cleaves covalent bonds between two sulfur atoms of non-adjacent amino acids in a polypeptide chain. Which level of protein structure is this drug targeting?

Question

BlackTom AI · Accepted Answer

Consider what disulfide bonds do in protein structure. A covalent S-S bond between cysteine residues stabilizes the folded shape of a single polypeptide chain, which is the hallmark of the protein's tertiary structure.

Option a: Primary. This level refers to the linear amino acid sequence; a disulfide bond between distant cysteines does not change the sequence itself, so this option is off the mark.

Option b: Secondary. This level describes local structures like alpha helices and beta sheets stabilized mainly by hydrogen bonds, not by covalent disulfide linkages between distant residues, so this is incorrect.

Option c: Tertiary. Correct, because the formation or disruption of disulfide bonds between non-adjacent cysteines within the same chain directly affects the overall 3D conformation of the polypeptide, i.e., its tertiary structure.

Option d: Quaternary. This level involves the arrangement and interactions between multiple polypeptide chains in a multimeric protein; since the question specifies a bond between residues within a single chain, targeting quaternary structure would require inter-chain crosslinks, which isn’t implied here.

A new drug is developed which selectively cleaves covalent bonds between two sulfur atoms of non-adjacent amino acids in a polypeptide chain. Which level of protein structure is this drug targeting?单项选择题

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