Linked Life Data

15458632

Source:http://linkedlifedata.com/resource/pubmed/id/15458632

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2004-10-1
pubmed:abstractText
The diffusion-collision model (DCM) is applied to the folding kinetics of protein L and protein G. In the DCM, the two proteins are treated as consisting of two beta-hairpins and one alpha-helix, so that they are isomorphous with the three-helix bundle DCM model. In the absence of sequence dependent factors, both proteins would fold in the same way in the DCM, with the coalescence of the N-terminal hairpin and the helix slightly favored over the C-terminal hairpin and the helix because the former are closer together than the latter. However, sequence dependent factors make the N-terminal hairpin of protein L and the C-terminal hairpin of protein G more stable in the ensemble of unfolded conformations. This difference in the stabilities gives rise to the difference in the calculated folding behavior, in agreement with experiment.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0969-2126
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Elsevier Ltd.
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1833-45
pubmed:dateRevised
2005-12-26
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The role of sequence and structure in protein folding kinetics; the diffusion-collision model applied to proteins L and G.
pubmed:affiliation
Structural Bioinformatics Group, Department of Biological Sciences, Biochemistry Building, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom.
pubmed:publicationType
Journal Article