What is the catalytic triad of chymotrypsin? Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytic triad and the significance of the oxyanion hole.
Q: Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is…
A: Peptide bond formation- A peptide bond is a chemical bond formed between two molecules when the…
Q: Write a balanced equation showing peptide bond formation between threonine and aspartate.
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Q: An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl…
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Q: Draw the structural formula for the pentapeptide segment being synthesized. (Val-Thr-Arg-Pro-Glu)…
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Q: Draw the mechanism for the hydrolysis of the peptide bonds of aspartame. Draw all arrows
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Q: How many peptide bonds in this peptide chain LEU-ILE-LEU?
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Q: the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed…
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Q: Draw the structure of Pro-Leu-Glu at physiological pH (7.4).
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Q: Show the steps involved in a Merrifield synthesis of Phe-Ala-Val.
A: In the Merrifield solid phase method, the synthesis of peptide is forwarded with the growing amino…
Q: Apamine is a small protein toxin present in the venom of the honey- bee. It has the sequence…
A: Apamin is an 18-residue bee venom peptide with the sequence CNCKAPETALCARRCQQH-amide. It is an 18…
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- Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is thermodynamically favorable. Would you expect chymotrypsin to catalyze peptide bond formation? Explain.Under certain conditions, peptide bond formation is more thermodynamically favorable than peptide bond hydrolysis. Would you expect chymotrypsin to catalyze peptide bond formation?What is the difference between an enol phosphate and a normal phosphate ester that gives PEP such a high phosphoryl group transfer potential?
- describe a detailed experimental procedure for the chemical synthesis of proteins with the α-ketoacid hydroxylamine (KAHA ligation), using (S)-5-oxaproline (Opr) as a key building block.Draw structural formulas for the products obtained when the tripeptide Thr-Leu-Ile undergoes complete hydrolysis under acidic conditionsIdentify the structure of the predominant form of the pentapeptide at pH = 12 if there is a pentapeptide Ile-Lys-Asp-Phe-Gly
- What peptides are expected to be produced when α-melanotropin is cleaved by (a) trypsin, (b) cyanogen bromide, or (c) thermolysin? (as shown)Individuals with phenylketonuria (PKU) are sensitive to phenylalanine in their diet. Why is a warning on foods containing aspartame (L-aspartyl-l-phenylalanine methyl ester) of concern to individuals with PKU?Draw the mechanism for the hydrolysis of the peptide bonds of aspartame. Draw all arrows
- An inhibitor that specifically labels chymotrypsin at histidine 57 is Ntosylamido-l-phenylethyl chloromethyl ketone. How would you modify the structure of this inhibitor to label the active site of trypsin?With the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl chloromethylketone. How would you modify the structure of this inhibitor tolabel the active site of trypsin?