Linked Life Data

18800837

Source:http://linkedlifedata.com/resource/pubmed/id/18800837

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
2008-10-9
pubmed:abstractText
Molecular dynamics simulations, guided by experimental information (Zondlo et al. Biochemistry 2006, 45, 11945-11957) have been used successfully to reproduce experimental trends in binding affinities of variant p53 peptides with MDM2. Simulations reveal how the conformations of the peptides and the receptor modulate each other to optimize interactions. The conformations of the uncomplexed peptides are governed by a combination of helix and intrinsic disorder (in agreement with experiments), while in the complexed state two very different conformations can coexist. This yields very similar binding affinities, driven by either enthalpy or entropy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
130
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13514-5
pubmed:dateRevised
2009-1-22
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Multiple peptide conformations give rise to similar binding affinities: molecular simulations of p53-MDM2.
pubmed:affiliation
Bioinformatics Institute (A-STAR), 30 Biopolis Street, #07-01 Matrix, Singapore 138671.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't