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dc.contributor.authorMoal, Iain H.
dc.contributor.authorFernández-Recio, Juan
dc.contributor.otherBarcelona Supercomputing Center
dc.date.accessioned2016-03-17T14:46:03Z
dc.date.available2016-03-17T14:46:03Z
dc.date.issued2014-10-17
dc.identifier.citationMoal, Iain H.; Fernández-Recio, Juan. Comment on ‘protein–protein binding affinity prediction from amino acid sequence. "Bioinformatics", 17 Octubre 2014, vol. 31, núm. 4, p. 614-615.
dc.identifier.issn1367-4803
dc.identifier.urihttp://hdl.handle.net/2117/84646
dc.description.abstractPredicting the strength of interactions between globular proteins is a central and important topic in structural bioinformatics (Moal et al., 2013). The amino acid sequence represents the chemical bonding in a protein which, along with the solvent, dictates how it folds into an ensemble of thermally accessible states. In turn, structure specifies the strength and identity of its binding partners, by establishing the specific arrangements of intermolecular interactions and the intramolecular strain required to achieve them.
dc.description.sponsorshipIHM received funding from the People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme (FP7/2007-2013) under REA grant agreement PIEF-GA-2012-327899.
dc.format.extent2 p.
dc.language.isoeng
dc.subjectÀrees temàtiques de la UPC::Enginyeria biomèdica
dc.subject.lcshProtein-protein interactions
dc.subject.otherProtein–protein interactions
dc.subject.otherAmino acid sequence
dc.titleComment on ‘protein–protein binding affinity prediction from amino acid sequence
dc.typeArticle
dc.subject.lemacProteïnes--Enginyeria genètica
dc.identifier.doi10.1093/bioinformatics/btu682
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://bioinformatics.oxfordjournals.org/content/31/4/614.long
dc.rights.accessOpen Access
dc.description.versionPostprint (published version)
dc.relation.projectidinfo:eu-repo/grantAgreement/EC/FP7/327899/EU/Exploring the evolution of protein-protein interactions and their networks using biophysical models/EEPPIBM
upcommons.citation.publishedtrue
upcommons.citation.publicationNameBioinformatics
upcommons.citation.volume31
upcommons.citation.number4
upcommons.citation.startingPage614
upcommons.citation.endingPage615


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