Chymotrypsin is a digestive serine protease that preferentially cleaves peptide bonds after certain bulky hydrophobic residues, especially aromatic residues. Its binding pocket favours those side chains, while its catalytic machinery hydrolyses the adjacent peptide bond. It is produced as an inactive precursor, limiting unwanted digestion before activation. Sequence preference is conditional rather than an assurance that every matching site in a folded protein is equally accessible. [ref]
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