Linked Life Data

17173286

Source:http://linkedlifedata.com/resource/pubmed/id/17173286

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-3-27
pubmed:abstractText
The study of protein conformational dynamics is motivated in large part by a desire to understand the forces present at different sites throughout the molecular structure. The generalized order parameter determined by NMR spectroscopy has played a central role in the study of protein dynamics on the picosecond-nanosecond time scale. A modeling procedure is presented for analysis of the temperature dependence of the generalized order parameter that extends a previous analysis (Massi and Palmer, J Am Chem Soc 2003;125:11158-11159). As part of this procedure, the potential of mean force is characterized for the N-H bond vectors of the protein backbone. This procedure accounts for the observed temperature dependence of the generalized order parameter in a representative data set from the B1 domain of Streptococcal protein G (Seewald, Pichumani, Stowell, Tibbals, Regan, and Stone, Protein Sci 2000;9:1177-1193). The results indicate a general trend, in which the force constants associated with the potential of mean force decrease with increasing temperature. The analysis also provides evidence for variations in the potential of mean force for different secondary structural elements.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1097-0134
pubmed:author
pubmed:copyrightInfo
(c) 2006 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
796-803
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Temperature dependence of the NMR generalized order parameter.
pubmed:affiliation
Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati, Cincinnati, Ohio 45267-0524, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural