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- W2090979435 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." @default.
- W2090979435 created "2016-06-24" @default.
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- W2090979435 date "2014-11-04" @default.
- W2090979435 modified "2023-10-18" @default.
- W2090979435 title "Long-Range Correlated Dynamics in Intrinsically Disordered Proteins" @default.
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- W2090979435 doi "https://doi.org/10.1021/ja506820r" @default.
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