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Science 18 August 1995:
Vol. 269. no. 5226, pp. 959 - 962
DOI: 10.1126/science.7638618
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Articles

Science, Vol 269, Issue 5226, 959-962
Copyright © 1995 by American Association for the Advancement of Science

articles

Protein reaction kinetics in a room-temperature glass

SJ Hagen, J Hofrichter, and WA Eaton

Laboratory of Chemical Physics, National Institutes of Health, Bethesda, MD 20892-0520, USA.

Protein reaction kinetics in aqueous solution at room temperature are often simplified by the thermal averaging of conformational substates. These substates exhibit widely varying reaction rates that are usually exposed by trapping in a glass at low temperature. Here, it is shown that the solvent viscosity, rather than the low temperature, is primarily responsible for the trapping. This was demonstrated by placement of myoglobin in a glass at room temperature and subsequent observation of inhomogeneous reaction kinetics. The high solvent viscosity slowed the rate of crossing the energy barriers that separated the substates and also suppressed any change in the average protein conformation after ligand dissociation.


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