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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.
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Submitted on : Friday, March 13, 2015 - 8:19:41 AM
Last modification on : Friday, August 5, 2022 - 2:54:00 PM


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


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⟩



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