Linked Life Data

17292839

Source:http://linkedlifedata.com/resource/pubmed/id/17292839

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-2-12
pubmed:abstractText
We recently developed a theory for the rates of protein-protein association. The theory is based on the concept of a transition state, which separates the bound state, with numerous short-range interactions but restricted translational and rotational freedom, and the unbound state, with, at most, a small number of interactions but expanded configurational freedom. When not accompanied by large-scale conformational changes, protein-protein association becomes diffusion limited. The association rate is then predicted as k(a)=k(a)(0)exp(-DeltaG(el)(double dagger)/k(B)T), where DeltaG(el)(double dagger) is the electrostatic interaction free energy in the transition state, k(a)(0) is the rate in the absence of electrostatic interactions, and k(B)T is thermal energy. Here, this transition-state theory is used to predict the association rates of four protein complexes. The predictions for the wild-type complexes and 23 mutants are found to agree closely with experimental data over wide ranges of ionic strength.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-24
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Prediction of protein-protein association rates from a transition-state theory.
pubmed:affiliation
Department of Physics and Institute of Molecular Biophysics and School of Computational Science, Florida State University, Tallahassee, FL 32306, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural