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pubmed-article:12944263pubmed:abstractTextWe present a Monte Carlo study of a model protein with 54 amino acids that folds directly to its native three-helix-bundle state without forming any well-defined intermediate state. The free-energy barrier separating the native and unfolded states of this protein is found to be weak, even at the folding temperature. Nevertheless, we find that melting curves to a good approximation can be described in terms of a simple two-state system, and that the relaxation behavior is close to single exponential. The motion along individual reaction coordinates is roughly diffusive on timescales beyond the reconfiguration time for a single helix. A simple estimate based on diffusion in a square-well potential predicts the relaxation time within a factor of two.lld:pubmed
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pubmed-article:12944263pubmed:authorpubmed-author:FavrinGiorgio...lld:pubmed
pubmed-article:12944263pubmed:authorpubmed-author:IrbäckAndersAlld:pubmed
pubmed-article:12944263pubmed:authorpubmed-author:WallinStefanSlld:pubmed
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pubmed-article:12944263pubmed:pagination1457-65lld:pubmed
pubmed-article:12944263pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:12944263pubmed:year2003lld:pubmed
pubmed-article:12944263pubmed:articleTitleTwo-state folding over a weak free-energy barrier.lld:pubmed
pubmed-article:12944263pubmed:affiliationComplex Systems Division, Department of Theoretical Physics, Lund University, Sölvegatan 14A, SE-223 62 Lund, Sweden.lld:pubmed
pubmed-article:12944263pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12944263pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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