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Journal Article

Long-range correlated dynamics in intrinsically disordered proteins.

MPS-Authors
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Rezaei-Ghaleh,  N.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Fulltext (public)

2079513.pdf
(Publisher version), 2MB

Supplementary Material (public)

2079513_Suppl.pdf
(Supplementary material), 301KB

Citation

Parigi, G., Rezaei-Ghaleh, N., Giachetti, A., Becker, S., Fernandez, C., Blackledge, M., et al. (2014). Long-range correlated dynamics in intrinsically disordered proteins. Journal of the American Chemical Society, 136(46), 16201-16209. doi:10.1021/ja506820r.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-5CAE-D
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 alpha-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 alpha-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.