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Long-range correlated dynamics in intrinsically disordered proteins.

dc.contributor.authorPARIGI, Giacomo
dc.contributor.authorREZAEI-GHALEH, Nasrollah
hal.structure.identifierMagnetic Resonance Center
dc.contributor.authorGIACHETTI, Andrea
dc.contributor.authorBECKER, Stefan
hal.structure.identifierInstitut de Mécanique et d'Ingénierie de Bordeaux [I2M]
dc.contributor.authorFERNANDEZ, Claudio
hal.structure.identifierInstitut de biologie structurale [IBS - UMR 5075 ]
dc.contributor.authorBLACKLEDGE, Martin
hal.structure.identifierMax Planck Institute for Biophysical Chemistry [MPI-BPC]
dc.contributor.authorGRIESINGER, Christian
dc.contributor.authorZWECKSTETTER, Markus
dc.contributor.authorLUCHINAT, Claudio
dc.date.accessioned2021-05-14T09:57:44Z
dc.date.available2021-05-14T09:57:44Z
dc.date.issued2014-11-19
dc.identifier.issn0002-7863
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/77891
dc.description.abstractEnIntrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in α-synuclein, which are related to genetic forms of Parkinson's disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.title.enLong-range correlated dynamics in intrinsically disordered proteins.
dc.typeArticle de revue
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
bordeaux.journalJournal of the American Chemical Society
bordeaux.page16201-9
bordeaux.volume136
bordeaux.hal.laboratoriesInstitut de Mécanique et d’Ingénierie de Bordeaux (I2M) - UMR 5295*
bordeaux.issue46
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.institutionCNRS
bordeaux.institutionINRAE
bordeaux.institutionArts et Métiers
bordeaux.peerReviewedoui
hal.identifierhal-01131128
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01131128v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.date=2014-11-19&rft.volume=136&rft.issue=46&rft.spage=16201-9&rft.epage=16201-9&rft.eissn=0002-7863&rft.issn=0002-7863&rft.au=PARIGI,%20Giacomo&REZAEI-GHALEH,%20Nasrollah&GIACHETTI,%20Andrea&BECKER,%20Stefan&FERNANDEZ,%20Claudio&rft.genre=article


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