| pubmed-article:8327519 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8327519 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:8327519 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8327519 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:8327519 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
| pubmed-article:8327519 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:8327519 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8327519 | pubmed:dateCreated | 1993-8-6 | lld:pubmed |
| pubmed-article:8327519 | pubmed:abstractText | Monte Carlo simulations on a class of lattice models are used to probe the thermodynamics and kinetics of protein folding. We find two transition temperatures: one at T theta, when chains collapse from a coil to a compact phase, and the other at Tf (< T theta), when chains adopt a conformation corresponding to their native state. The kinetics are probed by several correlation functions and are interpreted in terms of the underlying energy landscape. The transition from the coil to the native state occurs in three distinct stages. The initial stage corresponds to a random collapse of the protein chain. At intermediate times tau c, during which much of the native structure is acquired, there are multiple pathways. For longer times tau r (>> tau c) the decay is exponential, suggestive of a late transition state. The folding time scale (approximately tau r) varies greatly depending on the model. Implications of our results for in vitro folding of proteins are discussed. | lld:pubmed |
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| pubmed-article:8327519 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8327519 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8327519 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8327519 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8327519 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8327519 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8327519 | pubmed:author | pubmed-author:ThirumalaiDD | lld:pubmed |
| pubmed-article:8327519 | pubmed:author | pubmed-author:CamachoC JCJ | lld:pubmed |
| pubmed-article:8327519 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8327519 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8327519 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:8327519 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8327519 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8327519 | pubmed:pagination | 6369-72 | lld:pubmed |
| pubmed-article:8327519 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
| pubmed-article:8327519 | pubmed:meshHeading | pubmed-meshheading:8327519-... | lld:pubmed |
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| pubmed-article:8327519 | pubmed:meshHeading | pubmed-meshheading:8327519-... | lld:pubmed |
| pubmed-article:8327519 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8327519 | pubmed:articleTitle | Kinetics and thermodynamics of folding in model proteins. | lld:pubmed |
| pubmed-article:8327519 | pubmed:affiliation | Institute for Physical Science and Technology, University of Maryland, College Park 20742. | lld:pubmed |
| pubmed-article:8327519 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8327519 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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