Linked Life Data

15212507

Source:http://linkedlifedata.com/resource/pubmed/id/15212507

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2004-6-23
pubmed:abstractText
Local protein backbone dynamics on time scales reaching up to milliseconds have been investigated using residual dipolar couplings (RDC) using an analytical description of conformational averaging under the influence of anisotropic peptide plane dynamics. We have applied this technique to RDC from protein G and find that sites in the alpha-helix exhibit overall higher-order parameters than loops, suggesting a high degree of conformational integrity even over this extended time period. The approach is shown to be stable when using data from a smaller number of alignment media. Order parameters derived from combinations of independent subsets of two and three of the five alignment media from protein G reveal results essentially identical to those from the complete data set. Structures of lysozyme determined at different crystal diffraction resolutions ranging from 0.9 to 2.1 A give similar dynamic parameters using this method, demonstrating robustness with respect to structural error.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7760-1
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Local dynamic amplitudes on the protein backbone from dipolar couplings: toward the elucidation of slower motions in biomolecules.
pubmed:affiliation
Institut de Biologie Structurale - Jean-Pierre Ebel C.N.R.S.-C.E.A.-UJF 41, rue Jules Horowitz - 38027 Grenoble Cedex - France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't