Journal Article DZNE-2020-03968

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Long-range correlated dynamics in intrinsically disordered proteins.

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2014
American Chemical Society Washington, DC

Journal of the American Chemical Society 136(46), 16201-16209 () [10.1021/ja506820r]

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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

Classification:

Contributing Institute(s):
  1. Structural Biology in Dementia (AG Zweckstetter)
Research Program(s):
  1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2014
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 Record created 2020-02-18, last modified 2024-03-21


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