The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does the R group of hlstidine have that may be important for the activity of enzymes? Explain
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The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does the R group of hlstidine have that may be important for the activity of enzymes? Explain
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- Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?Draw the structure of the pentapeptide aspartic acid-serine-lysineUglutamic acidUtyrosine. Assume that thefree -NH2 group is at the aspartic acid end of the peptide chain. Would this compound be more likely to dissolve inwateror in octane? Explain.
- A schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.How does the structure of chymotrypsin enable it to cleave only peptide bonds that are adjacent to aromatic R groups? Suppose a protease could only cleave adjacent to Lysine and Arginine; how would the structure of this protein differ from that of chymotrypsin?Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?
- Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…Carboxypeptidase, which sequentially removes carboxyl-terminal amino acid residues from its peptide substrates, is a single polypeptide of 307 amino acids. The two essential catalytic groups in the active site arefurnished by Arg 145 and Glu 270 .(a) If the carboxypeptidase chain were a perfect α helix, how far apart (in Å) would Arg 145 and Glu 270 be? (b) Explain how the two amino acid residues can catalyze a reaction occurring in the space of a few angstromsConsider a hexapeptide of the sequence thr asn glu trp lys gln. After complete hydrolysis, which amino acid would elute first from a cation exchange column at pH 7? O Asn O GIn Thr Glu O Trp O Lys
- In some proteins, the side chain of serine appears to undergo ionization. Explain why ionization would be facilitated by the presence of an aspartate residue nearby.Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.