When specific conditions are met, the creation of peptide bonds rather than the hydrolysis of peptide bonds is thermodynamically advantageous. Would you have predicted that chymotrypsin would be involved in peptide bond formation? Explain?
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When specific conditions are met, the creation of peptide bonds rather than the hydrolysis of peptide bonds is
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- Under certain conditions, peptide bond formation is more thermodynamically favorable than peptide bond hydrolysis. Would you expect chymotrypsin to catalyze peptide bond formation?Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is thermodynamically favorable. Would you expect chymotrypsin to catalyze peptide bond formation? Explain.Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.
- Which of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation stateIf phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work? Do not just say yes or no. Give a short explanation for this hypothetical situation.Compare and contrast the biological roles of the following amino acids the following pairs ofamino acids. Once you have documented these role state which member of the pair is most important and why.
- Must the amino acid residues in the active site be near each other along the polypeptide chain? Explain.Proteins are thermodynamically unstable. The ΔG of the hydrolysis of proteins is quite negative, yet proteins can be quite stable. Explain this apparent paradox. What does it tell you about protein synthesis?the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.
- Are the amino acid residues at the active site need to be in close proximity to one another throughout the polypeptide chain? Explain.H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14Using condensed structures, supply an outline of the mechanism for the formation of Gly-Gly in the human body. (Hint: It is not a simple condensation reaction).