Linked Life Data

15369343

Source:http://linkedlifedata.com/resource/pubmed/id/15369343

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2004-9-16
pubmed:abstractText
Side-chain 2H NMR relaxation data have been collected for the SH3 domain from the Fyn tyrosine kinase and analyzed with respect to sequence preference and per-residue solvent accessibility. Residues that are highly preferred at a given position show a tendency to be less mobile than average with a coefficient of correlation that is greater than that obtained when side-chain flexibility and solvent accessibility are compared. The same trend is observed for five of six additional proteins considered. This provides evidence for the existence of conserved structural features other than hydrophobic burial that govern side-chain motions. Through examination of an SH3 domain structural alignment, we identify side-chain hydrogen bonding of threonine residues and a specific secondary structural element as potential determinants of protein internal dynamics.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9004-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins.
pubmed:affiliation
Protein Engineering Network Centres of Excellence, University of Toronto, Toronto, Ontario, Canada M5S 1A8.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't