Trypsin and chymotrypsin are members of the family of serine…
Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at the C-terminal end of specific residues. The recognition of a particular residue (side chain specificity) is determined by the structure and properties of a binding pocket. For each of the enzymes above, describe the characteristics of the binding pocket needed to attract the side chain of the correct amino acid residue in the polypeptide chain to be cleaved. These characteristics are listed below. a) the size (long/short) and shape (narrow, wide), as well as b) the polarity (hydrophobic/hydrophilic/type of charge (+/-) if present) Blank #1: trypsin Blank #2: chymotrypsin
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