Enzyme specificity under dynamic control: A normal mode analysis of α-lytic protease
- 12 February 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 286 (1), 267-278
- https://doi.org/10.1006/jmbi.1998.2445
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Direct Observation of Protein Solvation and Discrete Disorder with Experimental Crystallographic PhasesScience, 1996
- Normal mode analysis of protein dynamicsCurrent Opinion in Structural Biology, 1994
- Structural basis for broad specificity in .alpha.-lytic protease mutantsBiochemistry, 1991
- Structural analysis of specificity: .alpha.-lytic protease complexes with analogs of reaction intermediatesBiochemistry, 1989
- Structural plasticity broadens the specificity of an engineered proteaseNature, 1989
- Serine protease mechanism: structure of an inhibitory complex of .alpha.-lytic protease and a tightly bound peptide boronic acidBiochemistry, 1987
- Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme.Proceedings of the National Academy of Sciences, 1985
- Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.Proceedings of the National Academy of Sciences, 1983
- Dynamics of ligand binding to heme proteinsJournal of Molecular Biology, 1979
- Molecular structure of the α-lytic protease from Myxobacter 495 at 2·8 Å resolutionJournal of Molecular Biology, 1979