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  Long-range correlated dynamics in intrinsically disordered proteins.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-5CAE-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-D731-C
Genre: Journal Article

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http://pubs.acs.org/doi/pdf/10.1021/ja506820r (Publisher version)
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 Creators:
Parigi, G., Author
Rezaei-Ghaleh, N.1, Author              
Giachetti, A., Author
Becker, S.2, Author              
Fernandez, C., Author
Blackledge, M., Author
Griesinger, C.2, Author              
Zweckstetter, M.1, Author              
Luchinat, C., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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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 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.

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Language(s): eng - English
 Dates: 2014-10-212014-11-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/ja506820r
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 136 (46) Sequence Number: - Start / End Page: 16201 - 16209 Identifier: -