B. Explain how two amino acid residues can form a peptide
bond
I was able to get A) in this but I don't seem to understand this
completely.
B. Explain how two amino acid residues can form a peptide bond I was able to...
How do amino acid residues Asp102, His 57, and Ser 195 participate in peptide bond hydrolysis as catalyzed by chymotrypsin?
1. Explain why polyaspartatic acid (a peptide containing only aspartic acid residues) does NOT form an alpha helix at pH 7.0 but can at pH 2. 6. 2. What kind of non-covalent interaction would the following pairs of amino acids have in the three dimensional structure of a protein at pH 7.0? a) His-Asp b) Tyr-Asp c) Val-Leu d) Trp-Gln 3. Explain how the difference in structure of hemoglobin and myoglobin contribute to their different functions.
(a) Draw three different amino acid residues connected by two peptide bonds. (b) label each residue (3-letter code is OK). (c) Note bonds that do not rotate with a star (d) Note bonds that do rotate with a semi-circle arrow, including those found in each side chain (e) Of the residues in your drawing, which one contributes most to the entropy of the polypeptide (assume an unfolded state)?
Indicate which of the amino acid residues in the following peptide sequence contains a group that has a negative charge for its most likely charge state at pH 10. Phe-Val-Pro-His-Trp-Asn-Cys-Thr-Asp Please explain in detail how you got the answer. thank you!
Which of the statements about peptide bonds are true? D A tripeptide contains three amino acid residues. Peptide bonds are ester linkages. Peptide bond formation is a hydrolysis reaction. O Peptides are polymers of amino acids. Peptide bonds form from nucleophilic attack by an a-carboxyl carbon atom on an electron pair of an a-amino nitrogen atom of another amino acid.
Show how amino acid residues in polypeptide chain can form ester, imino and thioester crosslinks in proteins.
Sanger's reagent is used A) to determine the amino acid sequence of a peptide. B) to determine the C-terminal amino acid of a peptide. C) to determine the isoelectric point of a peptide. D) to determine the number of amino acids in a peptide. E) to determine the N-terminal amino acid of a peptide. Ninhydrin is used A) to determine the N-terminal amino acid of a peptide. B) to sequence amino acids in a peptide. C) to detect amino acids...
The peptide bond in proteins is A. only found between proline residues. B. usually cis unl ess proline is the next amino acid. C. usually trans unless proline is the next amino acid. D. is planar because of steric hinderance. E. defines one of the angles used in the Ramachandran plot.
3. Amino acid analysis of a peptide seven residues long gave: Asp, Leu, Lys, Met, Phe, Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. Reaction with phenylisothiocyanate reagent yielded PTH-Phe c. Treatment with chymotrypsin yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free lysine. What is the...
The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state (protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme.