PARIGI, Giacomo; REZAEI-GHALEH, Nasrollah; GIACHETTI, Andrea; BECKER, Stefan; FERNANDEZ, Claudio; BLACKLEDGE, Martin; GRIESINGER, Christian; ZWECKSTETTER, Markus; LUCHINAT, Claudio

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PARIGI, Giacomo

REZAEI-GHALEH, Nasrollah

GIACHETTI, Andrea
Magnetic Resonance Center

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Journal of the American Chemical Society. 2014-11-19, vol. 136, n° 46, p. 16201-9

American Chemical Society

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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.< Réduire

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Long-range correlated dynamics in intrinsically disordered proteins.

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