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1978). It seems that tandem duplication in pepsin allowed the creation of a binding site cleft. Members of the chymotrypsin family of proteases are composed of two homologous ͱ-barrel domains packed together asymmetrically. The important residues for catalysis are His57, Asp102, and Ser195. The domain interface forms the active site with the first two catalytic residues on the N-terminal barrel and the last one on the C-terminal barrel. 4 A˚ (McLachlan, 1979). This suggests that chymotrypsin evolved by tandem duplication, although no detectable sequence similarity remains.

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