Linked Life Data

12069627

Source:http://linkedlifedata.com/resource/pubmed/id/12069627

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-6-18
pubmed:abstractText
All-atom molecular dynamics simulations of proteins in solvent are now able to realistically map the protein-unfolding pathway. The agreement with experiments probing both folding and unfolding suggests that these simulated unfolding events also shed light on folding. The simulations have produced detailed models of protein folding transition, intermediate, and denatured states that are in both qualitative and quantitative agreement with experiment. The various studies presented here highlight how such simulations both complement and extend experiment.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0001-4842
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
422-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Molecular dynamics simulations of the protein unfolding/folding reaction.
pubmed:affiliation
Department of Medicinal Chemistry, University of Washington, Seattle, Washington 98195-7610, USA. Daggett@u.wahington.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review