Structures of Two Thermolysin-Inhibitor Complexes That Differ by a Single Hydrogen Bond
- 30 January 1987
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 235 (4788) , 571-574
- https://doi.org/10.1126/science.3810156
Abstract
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.This publication has 16 references indexed in Scilit:
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