What could be the reason why hydroxylation of proline residues is critical to the structural integrity of collagen? Select the correct response The hydroxyl moities in Pro form disulfide bonds which stabilize collagen structure. The hydroxyl moities in Pro form ionic bonds (salt bridges) which stabilize collagen structure. The hydroxyl moities in Pro form hydrophobic interactions which stabilize collagen structure. The hydroxyl moities in Pro form peptide bonds which stabilize collagen structure. The hydroxyl moities in Pro form H-bonds which stabilize collagen structure.

What could be the reason why hydroxylation of proline residues is critical to the structural integrity of collagen? Select the correct response The hydroxyl moities in Pro form disulfide bonds which stabilize collagen structure. The hydroxyl moities in Pro form ionic bonds (salt bridges) which stabilize collagen structure. The hydroxyl moities in Pro form hydrophobic interactions which stabilize collagen structure. The hydroxyl moities in Pro form peptide bonds which stabilize collagen structure. The hydroxyl moities in Pro form H-bonds which stabilize collagen structure.

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter2: Cell Physiology

Section: Chapter Questions

Problem 5TAHL

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Similar questions

What is one feature of fibrillar collagen that contributes to its strength? They form crosslinks between glycine and alanine residues on adjacent collagens. They form crosslinks between lysine and hydroxylysine residues on one collagen molecule. They form crosslinks between glycine and alanine residues on one collagen molecule. They form crosslinks between lysine and hydroxylysine residues on adjacent collagen molecules.
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