Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond

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Science  30 Jan 1987:
Vol. 235, Issue 4788, pp. 571-574
DOI: 10.1126/science.3810156


The mode of binding to thermolysin of the ester analog Cbz-GlyP-(O)-Leu-Leu has been determined by x-ray crystallography and shown to be virtually identical (maximum difference 0.2 angstrom) with the corresponding peptide analog Cbz-GlyP-(NH)-Leu-Leu. The two inhibitors provide a matched pair of enzyme-inhibitor complexes that differ by 4.1 kilocalories per mole in intrinsic binding energy but are essentially identical except for the presence or absence of a specific hydrogen bond.

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