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  Local and global dynamics in intrinsically disordered synuclein.

Rezaei-Ghaleh, N., Parigi, G., Soranno, A., Holla, A., Becker, S., Schuler, B., et al. (2018). Local and global dynamics in intrinsically disordered synuclein. Angewandte Chemie International Edition, 57(46), 15262-15266. doi:10.1002/anie.201808172.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-0CEE-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-AF9B-A
Genre: Journal Article

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 Creators:
Rezaei-Ghaleh, N.1, Author              
Parigi, G., Author
Soranno, A., Author
Holla, A., Author
Becker, S.2, Author              
Schuler, B., Author
Luchinat, C., Author
Zweckstetter, M.1, 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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Free keywords: intrinsically disordered proteins; NMR spectroscopy; protein dynamics
 Abstract: Intrinsically disordered proteins experience a diverse spectrum of motions that are difficult to characterize with a single experimental technique. Here we combine high- and low-field nuclear spin relaxation, nanosecond fluorescence correlation spectroscopy (nsFCS) and long molecular dynamics simulations of alpha-synuclein, a paradigmatic IDP involved in Parkinson disease, to obtain a comprehensive picture of its conformational dynamics. The combined analysis shows that fast motions below 2 ns caused by local dihedral angle fluctuations and conformational sampling within and between Ramachandran substates decorrelate most of the backbone N-H orientational memory. However, slow motions with correlation times of up to ~13 ns from segmental dynamics are present throughout the alpha-synuclein chain, in particular in its C-terminal domain, and global chain reconfiguration occurs on a timescale of ~ 60 ns. Our study demonstrates that the combination of high- and low-field nuclear spin relaxation together with nsFCS and molecular dynamics simulations is a powerful strategy to determine residue-specific protein dynamics in IDPs at different time and length scales.

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Language(s): eng - English
 Dates: 2018-10-182018-11-12
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201808172
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 57 (46) Sequence Number: - Start / End Page: 15262 - 15266 Identifier: -