Long-range correlated dynamics in intrinsically disordered proteins.

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.
Type de document :
Article dans une revue
Journal of the American Chemical Society, American Chemical Society, 2014, 136 (46), pp.16201-9
Liste complète des métadonnées

http://hal.univ-grenoble-alpes.fr/hal-01131128
Contributeur : Frank Thomas <>
Soumis le : vendredi 13 mars 2015 - 08:19:41
Dernière modification le : samedi 22 septembre 2018 - 13:30:02

Identifiants

  • HAL Id : hal-01131128, version 1
  • PUBMED : 25331250

Collections

Citation

Giacomo Parigi, Nasrollah Rezaei-Ghaleh, Andrea Giachetti, Stefan Becker, Claudio Fernandez, et al.. Long-range correlated dynamics in intrinsically disordered proteins.. Journal of the American Chemical Society, American Chemical Society, 2014, 136 (46), pp.16201-9. 〈hal-01131128〉

Partager

Métriques

Consultations de la notice

152