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  Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

Lange, O. F., Lakomek, N.-A., Farès, C., Schröder, G. F., Walter, K. F. A., Becker, S., et al. (2008). Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution. Science, 320(5882), 1471-1475. doi:10.1126/science.1157092.

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 Creators:
Lange, Oliver F.1, Author
Lakomek, Nils-Alexander2, Author
Farès, Christophe2, Author           
Schröder, Gunnar F.1, Author
Walter, Korvin F. A.2, Author
Becker, Stefan2, Author
Meiler, Jens3, Author
Grubmüller, Helmut1, Author
Griesinger, Christian2, Author
de Groot, Bert L.1, Author
Affiliations:
1Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany, ou_persistent22              
2Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              
3Vanderbilt University Center for Structural Biology, Nashville, TN 37212, USA, ou_persistent22              

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 Abstract: Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.

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Language(s): eng - English
 Dates: 2008-06-13
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1157092
 Degree: -

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Title: Science
  Other : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 320 (5882) Sequence Number: - Start / End Page: 1471 - 1475 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1