1) What is the charge state of the peptide in pH7 water solution? a GKEAPLCKR
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- Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.Vasopressin: CYFQNCPRG Oxytocin: CYIQNCPLG Both of these peptides will react with reducing agents such as beta mercaptoethnol (BME). What side group reacts with this reducing agent? What does the fact that these peptides both react with BME tell you about the side groups and therefore this peptide?How many small peptide fragments will result if you treat the peptide Gly–Trp–Ala–Leu–Arg–Ala–Lys–Trp–Gly–Arg–Phe–His–Pro–Ala–Tyr with pepsin?
- The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme UTSAse (the arrow indicates the peptide bond cleaved in each case). Substrate Km(mM) kcat(s-1) PAPA↓G 4.0 26 PAPA↓A 1.5 37 PAPA↓F 0.64 18 what features of amino acid sequence dictate the specificity of the proteolytic cleavage? Large hydrophilic R-groups Large hydrophobic R-groups Neutral R-groups Small hydrophilic R-groups Large hydrophobic R-groups Negatively charged R-groups Positively charged R-groupsCalculate the pI for the following tri-peptide: Glu-Arg-LysInsulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the hormone activity is recovered. This is the level of activity expected for random pairing of cysteine residues to form disulfide bonds. How can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?
- Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net chargeWhat amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin
- Given this peptide chain:LYS – MET – ASP – THR – GLN – ARG- LYS – TRP – MET – LYS – GLU – VAL- ARGIf the first 5 amino acid residue are subjected to anion exchange chromatography, which amino acids will come NOT out of the column? Please explain.The following peptide that has been acetylated at the C-terminus: CH3C(O)-GEEGH-NH2 Plot the titration curve for pH as a function of mols NaOH added, indicating the relevant pKa values and the pI value on the graph, label all axes appropriately.Consider the following peptide sequence: Lys-Leu-Ile-Cys-Lys What is the net charge of this sequence at physiological pH? a. -2 b. +1 c. 0 d. -1 e. +2