Concept explainers
(a)
Interpretation:
The peptides obtained from the cleavage of given peptide chain by trypsin has to be given.
Concept introduction:
Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).
Endopeptidases cleave peptide bonds that are not at the end.
Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine and lysine.
(b)
Interpretation:
The peptides obtained from the cleavage of given peptide chain by chymotrypsin has to be given.
Concept introduction:
Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).
Endopeptidases cleave peptide bonds that are not at the end.
Chymotrypsin is an endopeptidase, which cleave the C-side peptide bond of amino acids that contain
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Essential Organic Chemistry, Global Edition
- A decapeptide has the following amino acid composition. Ala2, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides. Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala + Lys-Val-Phe + Val-Phe-Gly One round of Edman degradation yields a lysine phenylthiohydantoin. From this information, deduce the primary structure of this decapeptide.arrow_forwardIf a heptapeptide is made of Y-P-G-P-H-I-L amino acid sequence, what qualitative tests will give positive results when it is subjected to acid hydrolysis?arrow_forwardPredict the products P and Q formed when the following peptide is treated with the given reagient. HS. H₂N (b) (c) (d) HS P P OH H₂N. PhNCS DIPEA H₂N. X DH P + Q OH CHarrow_forward
- After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhy-dride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trparrow_forwardWhat fragments are produced when the peptide shown below is treated with trypsin? Gly-Arg-Val-Phe -Leu-Lys-Met-Trp-Pro-Tyr-Cys-Serarrow_forwardWhich of the following reagents can be used to cleave a tert-butoxycarbonyl (Boc) protecting group from a peptide? H₂/Pd CF3CO₂H Na₂CO3, H₂O LiAlH4 Barrow_forward
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- Consider the heptapeptide: ser-lys-met-leu-gly-tyr-asnarrow_forwardAnother method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected amino acid to a p-nitrophenyl ester.[2] Reaction of the p-nitrophenyl ester with an amino acid ester.a. Why does a p-nitrophenyl ester “activate” the carboxy group of the first amino acid to amide formation? b. Would a p-methoxyphenyl ester perform the same function? Why or why not?arrow_forwardCleavage of the following peptide with cyanogen bromide would result in the production of smaller peptides, whereas cleavage with trypsin would result in the production of Ala-Lys-Met-Glu-Asp-Cys-Ile-Phe-Met-Cys-Trp-Glu three, three one, two two, two three, twoarrow_forward
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