Article: A gradient-directed Monte Carlo approach for protein design

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TitleA gradient-directed Monte Carlo approach for protein design
AuthorsHu, X1
Hu, H1
Beratan, DN1
Yang, W1
Issue Date2010
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/33822
CitationJournal Of Computational Chemistry, 2010, v. 31 n. 11, p. 2164-2168 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jcc.21506
AbstractWe develop a new global optimization strategy, gradient-directed Monte Carlo (GDMC) sampling, to optimize protein sequence for a target structure using RosettaDesign. GDMC significantly improves the sampling of sequence space, compared to the classical Monte Carlo search protocol, for a fixed backbone conformation as well as for the simultaneous optimization of sequence and structure. As such, GDMC sampling enhances the efficiency of protein design. © 2010 Wiley Periodicals, Inc.
ISSN0192-8651
2011 Impact Factor: 4.583
2011 SCImago Journal Rankings: 0.332
DOIhttp://dx.doi.org/10.1002/jcc.21506
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorHu, X
dc.contributor.authorHu, H
dc.contributor.authorBeratan, DN
dc.contributor.authorYang, W
dc.date.accessioned2012-10-08T03:19:18Z
dc.date.available2012-10-08T03:19:18Z
dc.date.issued2010
dc.description.abstractWe develop a new global optimization strategy, gradient-directed Monte Carlo (GDMC) sampling, to optimize protein sequence for a target structure using RosettaDesign. GDMC significantly improves the sampling of sequence space, compared to the classical Monte Carlo search protocol, for a fixed backbone conformation as well as for the simultaneous optimization of sequence and structure. As such, GDMC sampling enhances the efficiency of protein design. © 2010 Wiley Periodicals, Inc.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationJournal Of Computational Chemistry, 2010, v. 31 n. 11, p. 2164-2168 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jcc.21506
dc.identifier.citeulike7686232
dc.identifier.doihttp://dx.doi.org/10.1002/jcc.21506
dc.identifier.epage2168
dc.identifier.issn0192-8651
2011 Impact Factor: 4.583
2011 SCImago Journal Rankings: 0.332
dc.identifier.issue11
dc.identifier.pmid20186860
dc.identifier.scopuseid_2-s2.0-77954251377
dc.identifier.spage2164
dc.identifier.urihttp://hdl.handle.net/10722/168466
dc.identifier.volume31
dc.languageeng
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/33822
dc.publisher.placeUnited States
dc.relation.ispartofJournal of Computational Chemistry
dc.relation.referencesReferences in Scopus
dc.subject.meshAmino Acids - Chemistry
dc.subject.meshComputational Biology - Methods
dc.subject.meshDrug Design
dc.subject.meshMonte Carlo Method
dc.subject.meshProtein Conformation
dc.subject.meshProtein Folding
dc.subject.meshProteins - Chemistry
dc.subject.meshThermodynamics
dc.titleA gradient-directed Monte Carlo approach for protein design
dc.typeArticle
Author Affiliations
  1. Duke University