Which modified amino acid is commonly found in collagen?

Question

BlackTom AI · Accepted Answer

We start by restating the prompt to frame what is being asked: Which modified amino acid is commonly found in collagen?

Option survey: The provided data includes an answer field with Hydroxyproline as the response, but there are no listed answer_options to evaluate alongside it. This means we cannot compare multiple choices in this instance, so we’ll base the discussion on the known fact and explain why Hydroxyproline is the classic answer for collagen composition.

Correct concept explanation: Hydroxyproline is a post-translationally modified amino acid formed by hydroxylation of proline residues within collagen polypeptides. This modification is crucial because the additional hydroxyl groups enable extensive hydrogen bonding and stabilize the characteristic triple-helix structure of collagen, giving it tensile strength in connective tissues. The enzymes prolyl hydroxylase and the presence of vitamin C (as a cofactor) are essential for this modification; deficiencies in vitamin C disrupt hydroxyproline formation and collagen stability, leading to conditions like scurvy.

Why the answer Hydroxyproline is correct in context: It is the well-established modified amino acid associated with collagen. Its hydroxylation state directly contributes to the structural integrity of collagen fibers, which is central to collagen’s function in skin, bone, cartilage, and connective tissues.

Why related or alternative choices (if they were present) might be incorrect: In typical multiple-choice questions about collagen composition, other modified amino acids such as hydroxylysine can also appear, but hydroxyproline is the most characteristic and abundant modified residue in collagen. If an option claimed something unrelated (for example, a non-modified amino acid or a modification not linked to collagen stability), it would be inaccurate. Likewise, stating that collagen lacks post-translational modifications would be false.

Additional context: Collagen’s stability relies on hydroxyproline content, which influences the thermal stability of the triple helix. This is distinct from other structural proteins where different post-translational modifications may play roles, but hydroxyproline remains a hallmark of collagen biology.

BIOT5621.36986.202530 Exam I Spring 2025 retry

Which modified amino acid is commonly found in collagen?

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