ParkinsonFranceV1, Main, Exploration, bibRecordById, Hal:hal-01131128

Long-range correlated dynamics in intrinsically disordered proteins.

Identifieur interne : 000744 ( Main/Exploration ); précédent : 000743; suivant : 000745

Long-range correlated dynamics in intrinsically disordered proteins.

Auteurs : Giacomo Parigi ; Nasrollah Rezaei-Ghaleh ; Andrea Giachetti [Italie] ; Stefan Becker ; Claudio Fernandez [France] ; Martin Blackledge [France] ; Christian Griesinger [Allemagne] ; Markus Zweckstetter ; Claudio Luchinat

Source :

Journal of the American Chemical Society [ 0002-7863 ] ; 2014-11-19.

RBID : Hal:hal-01131128

Abstract

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.

Url:

http://hal.univ-grenoble-alpes.fr/hal-01131128

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Hal, to step Corpus: 000638
to stream Hal, to step Curation: 000638
to stream Hal, to step Checkpoint: 000226
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to stream Main, to step Curation: 000744

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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   |étape=   Exploration
   |type=    RBID
   |clé=     Hal:hal-01131128
   |texte=   Long-range correlated dynamics in intrinsically disordered proteins.
}}

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	La maladie de Parkinson en France (serveur d'exploration)
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La maladie de Parkinson en France (serveur d'exploration)

Long-range correlated dynamics in intrinsically disordered proteins.

Long-range correlated dynamics in intrinsically disordered proteins.

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