8327519

Source:http://linkedlifedata.com/resource/pubmed/id/8327519

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0022702, umls-concept:C0026336, umls-concept:C0033684, umls-concept:C0039808, umls-concept:C0185026
pubmed:issue	13
pubmed:dateCreated	1993-8-6
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.
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-1201909, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-1552936, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-1643270, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-1716783, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-1729690, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-1749933, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-2207096, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-2329583, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-2333297, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-2385597, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-2611345, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-3293595, http://linkedlifedata.com/resource/pubmed/commentcorrection/8327519-4124164
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7505876
pubmed:citationSubset	IM
pubmed:status	MEDLINE
pubmed:month	Jul
pubmed:issn	0027-8424
pubmed:author	pubmed-author:CamachoC JCJ, pubmed-author:ThirumalaiDD
pubmed:issnType	Print
pubmed:day	1
pubmed:volume	90
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	6369-72
pubmed:dateRevised	2010-9-13
pubmed:meshHeading	pubmed-meshheading:8327519-Kinetics, pubmed-meshheading:8327519-Models, Chemical, pubmed-meshheading:8327519-Monte Carlo Method, pubmed-meshheading:8327519-Protein Folding, pubmed-meshheading:8327519-Thermodynamics
pubmed:year	1993
pubmed:articleTitle	Kinetics and thermodynamics of folding in model proteins.
pubmed:affiliation	Institute for Physical Science and Technology, University of Maryland, College Park 20742.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S.