| Home > Publications Database > Long-range correlated dynamics in intrinsically disordered proteins. |
| Journal Article | DZNE-2020-03968 |
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2014
American Chemical Society
Washington, DC
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Please use a persistent id in citations: doi:10.1021/ja506820r
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.
Keyword(s): Animals (MeSH) ; Chemical Phenomena (MeSH) ; Intrinsically Disordered Proteins: chemistry (MeSH) ; Intrinsically Disordered Proteins: genetics (MeSH) ; Intrinsically Disordered Proteins: metabolism (MeSH) ; Models, Molecular (MeSH) ; Mutation (MeSH) ; Protein Conformation (MeSH) ; Protons (MeSH) ; Temperature (MeSH) ; Water: chemistry (MeSH) ; alpha-Synuclein: chemistry (MeSH) ; alpha-Synuclein: genetics (MeSH) ; alpha-Synuclein: metabolism (MeSH) ; Intrinsically Disordered Proteins ; Protons ; alpha-Synuclein ; Water
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