Bialek, William and Onuchic, José Nelson (1988) Protein Dynamics and Reaction Rates: Mode-Specific Chemistry in Large Molecules. Proceedings of the National Academy of Sciences of the United States of America, 85 (16). pp. 5908-5912. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:BIApnas88
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Reactive events in proteins may be strongly coupled to a few specific modes of protein motion or they may couple nonspecifically to the dense continuum of protein and solvent modes. We summarize the evidence that at least some biologically important reactions can be described in terms of a few specific modes, and we propose experiments to quantify the strength of coupling to the continuum. We also show that large entropic effects--solvent ordering, for example--can be rigorously incorporated in few-mode models without losing mode specificity. Within our description, the dynamics that determine chemical reaction rates can be summarized by a small number of parameters directly related to spectroscopic and thermodynamic data. Mode specificity allows protein dynamics to contribute directly to the control and specificity of biochemical reaction rates.
|Additional Information:||Copyright © 1988 by the National Academy of Sciences. Communicated by John J. Hopfield, February 16, 1988. We thank P. Debrunner, J. Friedman, and E. Stern for teaching us about the experiments discussed above, and J.J. Hopfield for his comments on the manuscript. This work was supported in part by the Miller Institute for Basic Research, by the U.S. Public Health Service through a Biomedical Research Support Grant, by the Brazilian agency CNPq, and by the National Science Foundation through Grant PCM84-06049 and a Presidential Young Investigator Award. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.|
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|Deposited On:||29 Oct 2007|
|Last Modified:||26 Dec 2012 09:45|
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