Linked Life Data

15081803

Source:http://linkedlifedata.com/resource/pubmed/id/15081803

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-4-14
pubmed:abstractText
Recent work has shown that a beta-sandwich domain from the human muscle protein titin (TI I27) unfolds via more than one pathway, providing experimental evidence for a long-standing theoretical prediction in protein folding. Here we present a thermodynamic analysis of two transition states along different folding pathways for this protein. The unusual upwards curvature previously observed in the denaturant-dependent unfolding kinetics is increased at both high and low temperatures, indicating that the high denaturant pathway is becoming more accessible. The transition states in each pathway are structurally distinct and have very different heat capacities. Interestingly the nucleation-condensation pathway is dominant at all physiologically relevant temperatures, supporting the suggestion that pathways with diffuse rather than localised transition states have been selected for by evolution to prevent misfolding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
338
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
445-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Thermodynamic characterisation of two transition states along parallel protein folding pathways.
pubmed:affiliation
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't