Structural basis for broad specificity in .alpha.-lytic protease mutants
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00107a005
Reference51 articles.
1. Nitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexes
2. Phosphonamidates as transition-state analog inhibitors of thermolysin
3. Bevington, P. R. (1969) Data Reduction and Error Analysis for the Physical Sciences, pp92-118, McGraw-Hill, New York.
4. Serine protease mechanism: structure of an inhibitory complex of .alpha.-lytic protease and a tightly bound peptide boronic acid
5. Structural plasticity broadens the specificity of an engineered protease
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