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pubmed-article:12868108pubmed:abstractTextBy using distributed computing techniques and a supercluster of more than 20,000 processors we simulated folding of a 20-residue Trp Cage miniprotein in atomistic detail with implicit GB/SA solvent at a variety of solvent viscosities (gamma). This allowed us to analyze the dependence of folding rates on viscosity. In particular, we focused on the low-viscosity regime (values below the viscosity of water). In accordance with Kramers' theory, we observe approximately linear dependence of the folding rate on 1/gamma for values from 1-10(-1)x that of water viscosity. However, for the regime between 10(-4)-10(-1)x that of water viscosity we observe power-law dependence of the form k approximately gamma(-1/5). These results suggest that estimating folding rates from molecular simulations run at low viscosity under the assumption of linear dependence of rate on inverse viscosity may lead to erroneous results.lld:pubmed
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pubmed-article:12868108pubmed:authorpubmed-author:PandeVijayVlld:pubmed
pubmed-article:12868108pubmed:authorpubmed-author:ZagrovicBojan...lld:pubmed
pubmed-article:12868108pubmed:copyrightInfoCopyright 2003 Wiley Periodicals, Inc. J Comput Chem 24: 1432-1436, 2003lld:pubmed
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pubmed-article:12868108pubmed:volume24lld:pubmed
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pubmed-article:12868108pubmed:pagination1432-6lld:pubmed
pubmed-article:12868108pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:12868108pubmed:articleTitleSolvent viscosity dependence of the folding rate of a small protein: distributed computing study.lld:pubmed
pubmed-article:12868108pubmed:affiliationBiophysics Program and Department of Chemistry, Stanford University, Stanford, CA 94305, USA.lld:pubmed
pubmed-article:12868108pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12868108pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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