Ascorbic acid (vitamin C) serves as a reducing agent responsible for maintaining

Question

Ascorbic acid (vitamin C) serves as a reducing agent responsible for maintaining the activity of prolyl hydroxylase, the enzyme that catalyzes hydroxylation of proline residues within the collagen triple helix, which is required for helix stability. Deficiencies in vitamin C lead to scurvy, which causes extensive bruising, hemorrhages, and breakdown of supporting tissues. What is the role of hydroxyproline in collagen triple helices? Hydroxylated proline residues, but apparently not non-hydroxylated or unhydroxylated proline residues, stabilize the collagen triple helix. The hydroxyl groups of this amino acid form interchain hydrogen bonds that help stabilize the assembled triple-stranded helix. Non-Hydroxylated proline residues, but apparently not hydroxylated proline residues, stabilize the collagen triple helix. The carboxyl groups of this amino acid form interchain hydrogen bonds that help stabilize the assembled triple-stranded helix. Non-Hydroxylated proline residues, but apparently not hydroxylated proline residues, stabilize the collagen triple helix. The hydroxyl groups of this amino acid form interchain hydrogen bonds that help stabilize the assembled triple-stranded helix. Hydroxylated proline residues, but apparently not non-hydroxylated or unhydroxylated proline residues, stabilize the collagen triple helix. The carboxyl groups of this amino acid form interchain hydrogen bonds that help stabilize the assembled triple-stranded helix.

Explanation / Answer

Hydroxy proline and proline are essential for stability of collagen residues. Their presence allows collagen molecules to make sharp turns to increase their stability. The additional OH group in hydroxy proline is also involved in interchain hydrogen bonding. This will further increase the stability of collagen triple helix. Therefore, the answer for this question is the first option, hydroxylated proline residues, but apparently not non-hydroxylated and unhydroxylated proline residues stabilise the collagen triple helix. The hydroxyl group of this amino acid forms interchain hydrogen bonds that helps stabilise the assembled triple stranded helix.

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