How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms 1 1Edited by J. Thornton
- 1 November 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 303 (5) , 797-811
- https://doi.org/10.1006/jmbi.2000.4154
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Optical detection of cytochrome P450 by sensitizer-linked substratesProceedings of the National Academy of Sciences, 1999
- Molecular Dynamics Simulations of P450 BM3—;Examination of Substrate-Induced Conformational ChangeJournal of Biomolecular Structure and Dynamics, 1999
- Accessibility to internal cavities and ligand binding sites monitored by protein crystallographic thermal factorsProteins-Structure Function and Bioinformatics, 1998
- Ligand Binding: Molecular Mechanics Calculation of the Streptavidin-Biotin Rupture ForceScience, 1996
- P450s: Structural similarities and functional differencesThe FASEB Journal, 1996
- Improved Binding of Cytochrome P450cam Substrate Analogues Designed To Fill Extra Space in the Substrate Binding PocketBiochemistry, 1996
- Electrostatic Control of the Substrate Access Channel in Cytochrome P-450camBiochemistry, 1994
- Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobinJournal of the American Chemical Society, 1990
- A computational procedure for determining energetically favorable binding sites on biologically important macromoleculesJournal of Medicinal Chemistry, 1985
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983