Please use this identifier to cite or link to this item: https://research.matf.bg.ac.rs/handle/123456789/321
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dc.contributor.authorAkhila, Melarkode Vattekatteen_US
dc.contributor.authorNarwani, Tarun Jairajen_US
dc.contributor.authorFloch, Alineen_US
dc.contributor.authorMaljković, Mirjanaen_US
dc.contributor.authorBisoo, Soubikaen_US
dc.contributor.authorShinada, Nicolas Ken_US
dc.contributor.authorKranjc, Agataen_US
dc.contributor.authorGelly, Jean-Christopheen_US
dc.contributor.authorSrinivasan, Narayanaswamyen_US
dc.contributor.authorMitić, Nenaden_US
dc.contributor.authorde Brevern, Alexandre Gen_US
dc.date.accessioned2022-08-09T12:43:35Z-
dc.date.available2022-08-09T12:43:35Z-
dc.date.issued2020-
dc.identifier.issn10478477-
dc.identifier.urihttps://research.matf.bg.ac.rs/handle/123456789/321-
dc.description.abstractSequence - structure - function paradigm has been revolutionized by the discovery of disordered regions and disordered proteins more than two decades ago. While the definition of rigidity is simple with X-ray structures, the notion of flexibility is linked to high experimental B-factors. The definition of disordered regions is more complex as in these same X-ray structures; it is associated to the position of missing residues. Thus a continuum so seems to exist between rigidity, flexibility and disorder. However, it had not been precisely described. In this study, we used an ensemble of disordered proteins (or regions) and, we applied a structural alphabet to analyse their local conformation. This structural alphabet, namely Protein Blocks, had been efficiently used to highlight rigid local domains within flexible regions and so discriminates deformability and mobility concepts. Using an entropy index derived from this structural alphabet, we underlined its interest to measure these local dynamics, and to quantify, for the first time, continuum states from rigidity to flexibility and finally disorder. We also highlight non-disordered regions in the ensemble of disordered proteins in our study.en_US
dc.language.isoenen_US
dc.relation.ispartofJournal of structural biologyen_US
dc.subjectEntropyen_US
dc.subjectFlexibilityen_US
dc.subjectProtein structuresen_US
dc.subjectRigidityen_US
dc.subjectStructural alphabeten_US
dc.titleA structural entropy index to analyse local conformations in intrinsically disordered proteinsen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.jsb.2020.107464-
dc.identifier.pmid31978465-
dc.identifier.scopus2-s2.0-85078942728-
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/85078942728-
dc.contributor.affiliationInformatics and Computer Scienceen_US
dc.relation.volume210en_US
dc.relation.issue1en_US
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeArticle-
crisitem.author.deptInformatics and Computer Science-
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