Linked Life Data

18647046

Source:http://linkedlifedata.com/resource/pubmed/id/18647046

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-7-23
pubmed:abstractText
We present a novel technique, based on the principle of maximum entropy, for deriving the solvation energy parameters of amino acids from the knowledge of the solvent accessible areas in experimentally determined native state structures as well as high quality decoys of proteins. We present the results of detailed studies and analyze the correlations of the solvation energy parameters with the standard hydrophobic scale. We study the ability of the inferred parameters to discriminate between the native state structures of proteins and their decoy conformations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1089-7690
pubmed:author
pubmed:issnType
Electronic
pubmed:day
21
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
035102
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Inference of the solvation energy parameters of amino acids using maximum entropy approach.
pubmed:affiliation
Physics Department, Penn State University, 104 Davey Lab, University Park, Pennsylvania 16801, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't