Linked Life Data

17136269

Source:http://linkedlifedata.com/resource/pubmed/id/17136269

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
2006-11-30
pubmed:abstractText
Molecular dynamics simulation and normal mode analysis are used to calculate the vibrational density of states of dihydrofolate reductase complexed with nicotinamide adenine dinucleotide phosphate at 120 K and the results are compared with the experimental spectrum derived from inelastic neutron scattering. The simulation results indicate that the experimental spectrum arises from an average over proteins trapped in different conformations with structural differences mainly in the loop regions, and that these conformations have significantly different low-frequency (<20 cm(-1)) spectra. Thus, the experimentally measured spectrum is an average over the vibrational modes of different protein conformations and is thus inhomogeneously broadened. The implications of this broadening for future neutron scattering experiments and ligand binding calculations are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1463-9076
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5543-8
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Conformational heterogeneity and low-frequency vibrational modes of proteins.
pubmed:affiliation
Institut des Hautes Etudes Scientifiques, 35 route de Chartres, 91440, Bures sur Yvette, France.
pubmed:publicationType
Journal Article