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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 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…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 stateTrypsin contains a/an [aspartate/serine/histidine] in its specificity pocket to attract lysine and arginine side chains. It contains a potent nucleophilic [histidine/serine/aspartate] in its active site that is capable of attacking the electrophilic [carbon/nitrogen/oxygen] of the closest peptide bond. The [acyl-enzyme/specificity pocket/oxyanion] transition state is stabilized by the backbone amide hydrogens of glycine and serine. In this way, the enzyme is able to catalyze the [hydrolysis/ligation/metalysis/hydrogenation] of the peptide bond.
- Describe the catabolism of a the amino acid serine. Start with serine and end with ATP. Give the details of every step.Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?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 substitution of a Glutamate residue for Valine residue is a conservative substitution. TrueFalseGlycosylation is a major type of protein post-translational modification. Identify the amino acid that is joined to each monosaccharide by a glycosidic bond. glycoprotein A glycoprotein B glycoprotein C HA HO Н CH₂OH HO OH Н H CH₂OH Н ОН HO HN-C-CH3 о c=0 NHI -NH-C - CH2C-H ОН Н нн ОН НН CH2OH Он OH HO Н NH 1 С=0 -CH2-C-н NH C=0 LO-CH2-C-H NH A В сDraw the peptide formed between asparagine and histidine. H,N- -CH-C-OH H,N-CH-ċ-OH ČH2 ČH, N° NH2 -NH +
- If you were to mutate Ser195 in the catalytic triad of chymotrypsin to another amino acid, which amino acid change would you expect to have the least effect on chymotrypsin catalytic activity? O Ala O Val O Phe O Thr O LeuWhich amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6? alanine leucine lysine arginine phenylalanineDefine aminoacyl (A) site