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  Population shuffling of protein conformations.

Smith, C. A., Ban, D., Pratihar, S., Giller, K., Schwiegk, C., de Groot, B. L., et al. (2015). Population shuffling of protein conformations. Angewandte Chemie International Edition, 54(1), 207-210. doi:10.1002/anie.201408890.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-B9EA-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3715-5
Genre: Journal Article

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 Creators:
Smith, C. A., Author
Ban, D.1, Author              
Pratihar, S.1, Author              
Giller, K.1, Author              
Schwiegk, C.1, Author              
de Groot, B. L.2, Author              
Becker, S.1, Author              
Griesinger, C.1, Author              
Lee, D.1, Author              
Affiliations:
1Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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Free keywords: conformation; kinetics; protein dynamics; relaxation dispersion; thermodynamics
 Abstract: Motions play a vital role in the functions of many proteins. Discrete conformational transitions to excited states, happening on timescales of hundreds of microseconds, have been extensively characterized. On the other hand, the dynamics of the ground state are widely unexplored. Newly developed high-power relaxation dispersion experiments allow the detection of motions up to a one-digit microsecond timescale. These experiments showed that side chains in the hydrophobic core as well as at protein-protein interaction surfaces of both ubiquitin and the third immunoglobulin binding domain of proteinG move on the microsecond timescale. Both proteins exhibit plasticity to this microsecond motion through redistribution of the populations of their side-chain rotamers, which interconvert on the picosecond to nanosecond timescale, making it likely that this population shuffling process is a general mechanism.

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Language(s): eng - English
 Dates: 2014-11-062015-01-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201408890
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 54 (1) Sequence Number: - Start / End Page: 207 - 210 Identifier: -