Biochemistry: Concepts and Connections (2nd Edition)
Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 8, Problem 11P

The following data describe the catalysis of cleavage of peptide bonds small peptides by the enzyme elastase.
Chapter 8, Problem 11P, The following data describe the catalysis of cleavage of peptide bonds small peptides by the enzyme

The arrow indicates the peptide bond cleaved each case.

a. If a mixture of these three substrates was presented to elastase with the concentration of each peptide equal to 0.5 mM, which would be digested most rapidly? Which most slowly? (Assume enzyme present in excess.)
b. On basis of these data, suggest what features of amino acid sequence dictate the specificity of proteolytic cleavage by elastase.
c. Elastase is closely related to chymotrypsin. Suggest two kinds of amino acid residues you might expect to find in or near the active site.

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Considering the chemical characteristics of the amino acids valine and glutamic acid (see Figure 5.14), propose a possible explanation for the dramatic effect on protein function that occurs when valine is substituted for glutamic acid.
Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?
you were given an unknown peptide. Explain in detail how you would determine the amino acid sequence of this peptide by means of Edman degradation. (You can do this by showing how you would determine the N-terminal amino acid of the peptide shown below in figure 2 with Edman degradation.
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