Digestive enzymes have been used in the study of protein structure. Which of the following explains
The usefulness of trypsin and chymotrypsin in studies of protein structure?
A) efficiency as exopeptidases
B) high specificity for particular peptide bonds
C) high stability because of the presence of disulfide cross-links
D) high turnover rates
E) rapid digestion of proteins to yield amino acids and small oligopeptides

Question

Quizplus · Accepted Answer

Trypsin and chymotrypsin are useful in protein structure studies because they have high specificity for cleaving peptide bonds at specific amino acids, allowing for controlled digestion and analysis of protein fragments.  Trypsin and chymotrypsin are enzymes of a class referred to as endoproteases. Both of these enzymes hydrolyze the peptide bond in substrate proteins at very specific sequences of amino acids. Trypsin cleaves the peptide bond that is C-terminal to a lysine or arginine residue. Chymotrypsin cleaves the peptide bond on the C-terminal side of tyrosine, tryptophan, or phenylalanine. Thus, the products of trypsin and chymotrypsin cleavage indicate the presence and number of these specific amino acids in a target protein.

Digestive Enzymes Have Been Used in the Study of Protein