Multiple Choice
The activity of chymotrypsin drastically changes as the pH fluctuates in the relatively small range of pH 5-9. What amino acid residue in chymotrypsin's active site is most likely to be responsible for this effect of pH?
2
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8. Protein Function
Chymotrypsin
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The following polypeptide N-G-I-F-D-A-Y-G-N-T-W-R-A-P-C-F-V-A is cleaved by chymotrypsin to produce multiple peptide fragments. Based on the specificity of chymotrypsin cleavage, how many peptide fragments are produced?
A
2 peptide fragments.
B
3 peptides fragments.
C
4 peptide fragments.
D
5 peptide fragments.
E
6 peptide fragments.
F
No cleavage event occurs
Verified step by step guidance1
Identify the specificity of chymotrypsin: Chymotrypsin cleaves peptide bonds on the carboxyl side of aromatic amino acids such as phenylalanine (F), tryptophan (W), and tyrosine (Y).
Examine the given polypeptide sequence: N-G-I-F-D-A-Y-G-N-T-W-R-A-P-C-F-V-A.
Locate the aromatic amino acids in the sequence: F (phenylalanine), Y (tyrosine), and W (tryptophan).
Determine the cleavage sites: Chymotrypsin will cleave after each of these aromatic residues, resulting in cleavage after F, Y, and W.
Count the resulting peptide fragments: Each cleavage event increases the number of fragments by one. Therefore, if there are three cleavage sites, the polypeptide will be divided into four fragments.
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