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Effects of S5-S2 interface mutations on activity. A, detailed view of side chain contacts at the interface. B, comparison of the activities of wild-type and mutant proteases (assayed in detergent). In the lower panels, less protease (10%) was used to prevent substrate depletion (the reaction was ∼10 times slower under this condition). C, the relative activity (wild-type protease = 1) is based on the initial reaction rates calculated from the gels shown in B.
