Draw the structure of Phe-Ser-Met-Glu, and indicate where the peptide bonds are.
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- b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEUDescribe and recognize the 20 alpha amino acid structures and their side chains.
- Sketch a titration curve for the amino acid lysine,and indicate the pKa values for all titratable groups. Also indicatethe pH at which the amino acid has no net chargeAre amino acids other than the usual 20 amino acidsfound in proteins? If so, how are such amino acids incorporatedinto proteins? Give an example of such an amino acid and a protein in which it occurs.Draw a peptide containing ELPT amino acids at pH 7 and label the phi and psi bonds. What is the isometric point of the peptide?
- Draw the structural formulas of the following peptides, andshow which bond would be cleaved by chymotrypsin.a. trp-val-glyb. phe-ala-proCalculate the isoelectric point for each amino acid.a. asparagine: pKa (COOH) = 2.02; pKa (α-NH3+) = 8.80b. methionine: pKa (COOH) = 2.28; pKa (α-NH3+) = 9.21Draw the structure of a dipeptide containing the amino acidsalanine and tyrosine and outline the peptide bond.