pubmed-article:12944263 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12944263 | lifeskim:mentions | umls-concept:C1762617 | lld:lifeskim |
pubmed-article:12944263 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
pubmed-article:12944263 | lifeskim:mentions | umls-concept:C0173022 | lld:lifeskim |
pubmed-article:12944263 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12944263 | pubmed:dateCreated | 2003-8-28 | lld:pubmed |
pubmed-article:12944263 | pubmed:abstractText | We 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:12944263 | pubmed:language | eng | lld:pubmed |
pubmed-article:12944263 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12944263 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12944263 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12944263 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12944263 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12944263 | pubmed:month | Sep | lld:pubmed |
pubmed-article:12944263 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:12944263 | pubmed:author | pubmed-author:FavrinGiorgio... | lld:pubmed |
pubmed-article:12944263 | pubmed:author | pubmed-author:IrbäckAndersA | lld:pubmed |
pubmed-article:12944263 | pubmed:author | pubmed-author:WallinStefanS | lld:pubmed |
pubmed-article:12944263 | pubmed:author | pubmed-author:SamuelssonBjö... | lld:pubmed |
pubmed-article:12944263 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12944263 | pubmed:volume | 85 | lld:pubmed |
pubmed-article:12944263 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12944263 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12944263 | pubmed:pagination | 1457-65 | lld:pubmed |
pubmed-article:12944263 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:12944263 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12944263 | pubmed:articleTitle | Two-state folding over a weak free-energy barrier. | lld:pubmed |
pubmed-article:12944263 | pubmed:affiliation | Complex Systems Division, Department of Theoretical Physics, Lund University, Sölvegatan 14A, SE-223 62 Lund, Sweden. | lld:pubmed |
pubmed-article:12944263 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12944263 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12944263 | lld:pubmed |