Long-range correlated dynamics in intrinsically disordered proteins.
| dc.contributor.author | PARIGI, Giacomo | |
| dc.contributor.author | REZAEI-GHALEH, Nasrollah | |
| hal.structure.identifier | Magnetic Resonance Center | |
| dc.contributor.author | GIACHETTI, Andrea | |
| dc.contributor.author | BECKER, Stefan | |
| dc.contributor.author | FERNANDEZ, Claudio | |
| hal.structure.identifier | Institut de biologie structurale [IBS - UMR 5075 ] | |
| dc.contributor.author | BLACKLEDGE, Martin | |
| hal.structure.identifier | Max Planck Institute for Biophysical Chemistry [MPI-BPC] | |
| dc.contributor.author | GRIESINGER, Christian | |
| dc.contributor.author | ZWECKSTETTER, Markus | |
| dc.contributor.author | LUCHINAT, Claudio | |
| dc.date.accessioned | 2021-05-14T09:57:44Z | |
| dc.date.available | 2021-05-14T09:57:44Z | |
| dc.date.issued | 2014-11-19 | |
| dc.identifier.issn | 0002-7863 | |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/77891 | |
| dc.description.abstractEn | Intrinsically 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.iso | en | |
| dc.publisher | American Chemical Society | |
| dc.title.en | Long-range correlated dynamics in intrinsically disordered proteins. | |
| dc.type | Article de revue | |
| dc.subject.hal | Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM] | |
| bordeaux.journal | Journal of the American Chemical Society | |
| bordeaux.page | 16201-9 | |
| bordeaux.volume | 136 | |
| bordeaux.hal.laboratories | Institut de Mécanique et d’Ingénierie de Bordeaux (I2M) - UMR 5295 | * |
| bordeaux.issue | 46 | |
| bordeaux.institution | Université de Bordeaux | |
| bordeaux.institution | Bordeaux INP | |
| bordeaux.institution | CNRS | |
| bordeaux.institution | INRAE | |
| bordeaux.institution | Arts et Métiers | |
| bordeaux.peerReviewed | oui | |
| hal.identifier | hal-01131128 | |
| hal.version | 1 | |
| hal.origin.link | https://hal.archives-ouvertes.fr//hal-01131128v1 | |
| bordeaux.COinS | ctx_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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