Collagen is unusual in its amino acid composition and requires a wide variety of posttranslational modifications to convert it to a functional molecule. Because of the complexity of collagen synthesis, there are many diseases, resulting in structural weaknesses in connective tissue, caused by defects in the process. Scurvy leads to a less stable collagen lacking sufficient hydroxyproline. 4-Hydroxylation of specific prolyl residues during collagen synthesis requires all of the following except A. Fe2+ B. a specific amino acid sequence at the site of hydroxylation. C. ascorbic acid. D. co-hydroxylation of lysine . E. individual α-chains, not yet assembled into a triple helix.
Collagen is unusual in its amino acid composition and requires a wide variety of posttranslational modifications to convert it to a functional molecule. Because of the complexity of collagen synthesis, there are many diseases, resulting in structural weaknesses in connective tissue, caused by defects in the process. Scurvy leads to a less stable collagen lacking sufficient hydroxyproline. 4-Hydroxylation of specific prolyl residues during collagen synthesis requires all of the following except A. Fe2+ B. a specific amino acid sequence at the site of hydroxylation. C. ascorbic acid. D. co-hydroxylation of lysine . E. individual α-chains, not yet assembled into a triple helix.
Human Heredity: Principles and Issues (MindTap Course List)
11th Edition
ISBN:9781305251052
Author:Michael Cummings
Publisher:Michael Cummings
Chapter9: Gene Expression And Gene Regulation
Section: Chapter Questions
Problem 22QP: Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant...
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Collagen is unusual in its amino acid composition and requires a wide variety of posttranslational modifications to convert it to a functional molecule. Because of the complexity of collagen synthesis, there are many diseases, resulting in structural weaknesses in connective tissue, caused by defects in the process. Scurvy leads to a less stable collagen lacking sufficient hydroxyproline. 4-Hydroxylation of specific prolyl residues during collagen synthesis requires all of the following except
A. Fe2+
B. a specific amino acid sequence at the site of hydroxylation.
C. ascorbic acid.
D. co-hydroxylation of lysine .
E. individual α-chains, not yet assembled into a triple helix.
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