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Dynamical theory of activated processes in globular proteins

Authors :
Michael Pear
Martin Karplus
Scott H. Northrup
J. A. McCammon
C. Y. Lee
Source :
Proceedings of the National Academy of Sciences of the United States of America. 79(13)
Publication Year :
1982

Abstract

A method is described for calculating the reaction rate in globular proteins of activated processes such as ligand binding or enzymatic catalysis. The method is based on the determination of the probability that the system is in the transition state and of the magnitude of the reactive flux for transition-state systems. An "umbrella sampling" simulation procedure is outlined for evaluating the transition-state probability. The reactive flux is obtained from an approach described previously for calculating the dynamics of transition-state trajectories. An application to the rotational isomerization of an aromatic ring in the bovine pancreatic trypsin inhibitor is presented. The results demonstrate the feasibility of calculating rate constants for reactions in proteins and point to the importance of solvent effects for reactions that occur near the protein surface.

Details

ISSN :
00278424
Volume :
79
Issue :
13
Database :
OpenAIRE
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Accession number :
edsair.doi.dedup.....1d5d5f64979709f4a76a5d548fe99eb4