Question

Aspartate proteases display a variety of substrate specificities, but normally they are most active in cleavage of peptide bonds:
a. on the carboxyl side of the basic amino acids.
b. on the carboxyl side of aromatic amino acids.
c. on the carboxyl side of small, neutral residues.
d. between two hydrophobic amino acid residues.
e. none of the above.

Answer

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