Linked Life Data

11397137

Source:http://linkedlifedata.com/resource/pubmed/id/11397137

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-6-8
pubmed:abstractText
We refine a protein model that reproduces fundamental aspects of protein thermodynamics. The model exhibits two transitions, hot and cold unfolding. The number of relevant parameters is reduced to three: (1) binding energy of folding relative to the orientational energy of bound water, (2) ratio of degrees of freedom between the folded and unfolded protein chain, and (3) the number of water molecules that can access the hydrophobic parts of the protein interior upon unfolding. By increasing the number of water molecules in the model, the separation between the two peaks in the heat capacity curve comes closer, which is more consistent with experimental data. In the end we show that if we, as a speculative assumption, assign only two distinct energy levels for the bound water molecules, better correspondence with experiments can be obtained.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-5193
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
210
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
367-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Thermodynamical implications of a protein model with water interactions.
pubmed:affiliation
Department of Physics, Norwegian University of Science and Technology, Trondheim, NO-7491, Norway. audun.bakk@phys.ntnu.no
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't