Linked Life Data

17419610

Source:http://linkedlifedata.com/resource/pubmed/id/17419610

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2007-4-26
pubmed:abstractText
By suitably extending a recent approach [Bussi, G.; et al. J. Am. Chem. Soc. 2006, 128, 13435] we introduce a powerful methodology that allows the parallel reconstruction of the free energy of a system in a virtually unlimited number of variables. Multiple metadynamics simulations of the same system at the same temperature are performed, biasing each replica with a time-dependent potential constructed in a different set of collective variables. Exchanges between the bias potentials in the different variables are periodically allowed according to a replica exchange scheme. Due to the efficaciously multidimensional nature of the bias the method allows exploring complex free energy landscapes with high efficiency. The usefulness of the method is demonstrated by performing an atomistic simulation in explicit solvent of the folding of a Triptophane cage miniprotein. It is shown that the folding free energy landscape can be fully characterized starting from an extended conformation with use of only 40 ns of simulation on 8 replicas.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4553-9
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
A bias-exchange approach to protein folding.
pubmed:affiliation
International School for Advanced Studies (SISSA/ISAS), Via Beirut 2-4, Trieste, Italy, and Nanochemistry Research Institute, Curtin University of Technology, GPO Box U1987, Perth 6845, Western Australia. piana@power.curtin.edu.au
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't