000279302 001__ 279302
000279302 005__ 20210129221031.0
000279302 0247_ $$2doi$$a10.1002/prot.24939
000279302 0247_ $$2ISSN$$a0887-3585
000279302 0247_ $$2ISSN$$a1097-0134
000279302 0247_ $$2WOS$$aWOS:000399417500023
000279302 0247_ $$2altmetric$$aaltmetric:4590309
000279302 0247_ $$2pmid$$apmid:26441154
000279302 037__ $$aFZJ-2015-07317
000279302 082__ $$a540
000279302 1001_ $$0P:(DE-Juel1)145868$$aDella Corte, Dennis$$b0
000279302 245__ $$aProtein structure refinement with adaptively restrained homologous replicas
000279302 260__ $$aNew York, NY$$bWiley-Liss$$c2016
000279302 3367_ $$2DRIVER$$aarticle
000279302 3367_ $$2DataCite$$aOutput Types/Journal article
000279302 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1552653307_21952
000279302 3367_ $$2BibTeX$$aARTICLE
000279302 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000279302 3367_ $$00$$2EndNote$$aJournal Article
000279302 520__ $$aA novel protein refinement protocol is presented which utilizes molecular dynamics (MD) simulations of an ensemble of adaptively restrained homologous replicas. This approach adds evolutionary information to the force field and reduces random conformational fluctuations by coupling of several replicas. It is shown that this protocol refines the majority of models from the CASP11 refinement category and that larger conformational changes of the starting structure are possible than with current state of the art methods. The performance of this protocol in the CASP11 experiment is discussed. We found that the quality of the refined model is correlated with the structural variance of the coupled replicas, which therefore provides a good estimator of model quality. Furthermore, some remarkable refinement results are discussed in detail.
000279302 536__ $$0G:(DE-HGF)POF3-551$$a551 - Functional Macromolecules and Complexes (POF3-551)$$cPOF3-551$$fPOF III$$x0
000279302 536__ $$0G:(DE-Juel1)jics66_20140501$$aCritical Assessment of Protein Structure Prediction 11 (jics66_20140501)$$cjics66_20140501$$fCritical Assessment of Protein Structure Prediction 11$$x1
000279302 588__ $$aDataset connected to CrossRef
000279302 7001_ $$0P:(DE-Juel1)131565$$aWildberg, André$$b1
000279302 7001_ $$0P:(DE-Juel1)132018$$aSchröder, Gunnar$$b2$$eCorresponding author
000279302 773__ $$0PERI:(DE-600)1475032-6$$a10.1002/prot.24939$$gp. n/a - n/a$$nS1$$p302-313$$tProteins$$v84$$x0887-3585$$y2016
000279302 8564_ $$uhttps://juser.fz-juelich.de/record/279302/files/Protein%20structure%20refinement%20with%20adaptively%20restrained%20homologous%20replicas_2016.pdf$$yRestricted
000279302 8564_ $$uhttps://juser.fz-juelich.de/record/279302/files/Protein%20structure%20refinement%20with%20adaptively%20restrained%20homologous%20replicas_2016.gif?subformat=icon$$xicon$$yRestricted
000279302 8564_ $$uhttps://juser.fz-juelich.de/record/279302/files/Protein%20structure%20refinement%20with%20adaptively%20restrained%20homologous%20replicas_2016.jpg?subformat=icon-1440$$xicon-1440$$yRestricted
000279302 8564_ $$uhttps://juser.fz-juelich.de/record/279302/files/Protein%20structure%20refinement%20with%20adaptively%20restrained%20homologous%20replicas_2016.jpg?subformat=icon-180$$xicon-180$$yRestricted
000279302 8564_ $$uhttps://juser.fz-juelich.de/record/279302/files/Protein%20structure%20refinement%20with%20adaptively%20restrained%20homologous%20replicas_2016.jpg?subformat=icon-640$$xicon-640$$yRestricted
000279302 8564_ $$uhttps://juser.fz-juelich.de/record/279302/files/Protein%20structure%20refinement%20with%20adaptively%20restrained%20homologous%20replicas_2016.pdf?subformat=pdfa$$xpdfa$$yRestricted
000279302 909CO $$ooai:juser.fz-juelich.de:279302$$pVDB
000279302 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)145868$$aForschungszentrum Jülich GmbH$$b0$$kFZJ
000279302 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132018$$aForschungszentrum Jülich GmbH$$b2$$kFZJ
000279302 9131_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000279302 9141_ $$y2016
000279302 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000279302 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000279302 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bPROTEINS : 2014
000279302 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000279302 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000279302 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000279302 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000279302 915__ $$0StatID:(DE-HGF)0550$$2StatID$$aNo Authors Fulltext
000279302 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000279302 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000279302 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000279302 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000279302 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000279302 920__ $$lyes
000279302 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000279302 9201_ $$0I:(DE-82)080012_20140620$$kJARA-HPC$$lJARA - HPC$$x1
000279302 980__ $$ajournal
000279302 980__ $$aVDB
000279302 980__ $$aI:(DE-Juel1)ICS-6-20110106
000279302 980__ $$aI:(DE-82)080012_20140620
000279302 980__ $$aUNRESTRICTED
000279302 981__ $$aI:(DE-Juel1)IBI-7-20200312