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Abnormalities in the synthesis or structure of collagen cause dysfunctions in cardiac organs, bone, skin, joints, and cyes. Problems may result from abnormal collagen genes, abnormal posttranslational modifications of collagen, or deficiency of cofactors needed by enzymes responsible for posttranslational modifications. Scurvy, a lack of vitamin \(\mathrm{C},\) is an example of the last type. The formation of covalent cross-links in collagen A. occurs during synthesis of the peptide chain. B. uses hydroxyproline. C. involves glycine residues. D. requires conversion of some \(\varepsilon\) -amino groups of lysine to \(\delta\) -aldchydes. E. all of the above.

Short Answer

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A. Cross-link formation occurs during the synthesis of the peptide chain. B. Covalent cross-link formation uses hydroxyproline. C. The cross-link formation in collagen involves glycine residues. D. Cross-link formation requires conversion of some ε-amino groups of lysine to δ-aldehydes. E. All of the above statements are correct. Answer: D. Cross-link formation in collagen requires conversion of some ε-amino groups of lysine to δ-aldehydes.

Step by step solution

01

Cross-link formation in collagen

Covalent cross-links in collagen are essential for stability. The formation of these cross-links involves the hydroxylysine and lysine residues present in the polypeptide chains.
02

Check Option A

Option A says cross-link formation occurs during synthesis of the peptide chain. However, cross-links in collagen happen after the peptide chain is synthesized, via post-translational modifications. Therefore, option A is incorrect.
03

Check Option B

Option B states that covalent cross-link formation uses hydroxyproline. Although hydroxyproline has an essential role in stabilizing collagen structure, it is not involved directly in the formation of cross-links. Instead, cross-link formation involves hydroxylysine and lysine. So option B is incorrect.
04

Check Option C

Option C says that the cross-link formation in collagen involves glycine residues. Although glycine makes up a significant portion of collagen's structure, it is not involved in the formation of cross-links. Hence, option C is incorrect.
05

Check Option D

Option D states that cross-link formation requires conversion of some ε-amino groups of lysine to δ-aldehydes. This statement is correct; cross-links are formed through the lysyl oxidase enzyme, which converts some lysine and hydroxylysine residues to aldehydes that can then react to form cross-links. Therefore, option D is correct.
06

Check Option E

Option E says that all of the above statements are correct. As we have evaluated the options A, B, and C are incorrect; thus, option E cannot be correct either. The correct answer is D. Cross-link formation in collagen requires conversion of some ε-amino groups of lysine to δ-aldehydes.

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Most popular questions from this chapter

Many pathological hyperlipoproteinemias result from abnormalitics in the rates of synthesis or clearance of lipoproteins in the blood. They are usually characterized by elevated levels of cholesterol and/or triacylglycerols in the blood. Type I has very high plasma triacylglycerol levels \((>1000 \mathrm{g} / \mathrm{dL})\) because of an accumulation of chylomicrons. Type II (familial hypercholesterolemia) has elevated cholesterol, specifically in the form of LDL. Another abnormality of lipoproteins is hypolipoproteinemia in which lipoproteins are not formed because of the inability to make a particular apoprotein. In abecalipoproteinemia chylomicrons, VLDL and LDL are absent from the blood. Which of the following is correct? A. In this discase, no apolipoproteins are synthesized. B. If the blood from these individuals were centrifuged, the lipid bands would be found primarily in the upper half of the tube. C. Failure to synthesize apolipoprotein ApoB-100 and ApoB-48 would account for the pattern shown in this disease. D. Apolipoproteins are composed mostly of \(\beta\) structure. E. All of the above.

Similar arrangements of secondary structural motifs are often observed in the fold structure of protein domains. Which of the following is correct? A. Superfolds are similar structures from proteins related by function or evolution from the same primordial gene. B. Folds must be either all \(\alpha\) or all \(\beta\) C. There is only one type of \(\beta\) domain. D. If a protein has more than one domain, all domains are identical. E. A common fold has a central \(\beta\) -barrel with the strands connected by \(\alpha\) -helices around the outside.

Abnormalities in the synthesis or structure of collagen cause dysfunctions in cardiac organs, bone, skin, joints, and cyes. Problems may result from abnormal collagen genes, abnormal posttranslational modifications of collagen, or deficiency of cofactors needed by enzymes responsible for posttranslational modifications. Scurvy, a lack of vitamin \(\mathrm{C},\) is an example of the last type. In collagen: A. intrachain hydrogen bonding stabilizes the native structure. B. three chains with polyproline type helical conformation can wind about one another to form a superhelix because of the structure of glycine. C. the \(\varphi\) angles contributed by proline are free to rotate. D. regions of superhelicity comprise the entire structure except for the \(N\) - and \(C\) -termini. E. crosslinks berween triple helices form after lysine is converted to allysine.

Chaperone proteins A. all require ATP to exert their effect. B. cleave incorrect disulfide bonds, allowing correct ones to subsequently form. C. guide the folding of polypeptide chains into patterns that would be thermodynamically unstable without the presence of chaperones. D. of the Hsp70 class are involved in transport of proteins across mitochondrial and endoplasmic reticulum membranes. E. act only on fully synthesized polypeptide chains.

In an \(\alpha\) -helix, A. side-chain groups can align to give a polar face. B. cach peptide bond forms two hydrogen bonds. C. there are 3.6 amino acids per turn. D. all of the above. E. none of the above.

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