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  Residual dipolar couplings as a tool to study molecular recognition of ubiquitin

Lakomek, N.-.-A., Lange, O. F., Walter, K. F. A., Farès, C., Egger, D., Lunkenheimer, P., et al. (2008). Residual dipolar couplings as a tool to study molecular recognition of ubiquitin. Biochemical Society Transactions, 36(6), 1433-1437. doi:10.1042/BST0361433.

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 Creators:
Lakomek, Nils -Alexander1, Author           
Lange, Oliver F.2, Author
Walter, Korvin F. A.1, Author
Farès, Christophe3, Author           
Egger, Dalia4, Author
Lunkenheimer, Peter4, Author
Meiler, Jens5, Author
Grubmüller, Helmut2, Author
Becker, Stefan1, Author
de Groot, Bert L.2, Author
Griesinger, Christian1, Author           
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Department for Theoretical and Computational Biophysics, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany, , ou_persistent22              
3University Health Network, Max Bell Research Center, Toronto, Canada, ou_persistent22              
4Department for Experimental Physics V, University of Augsburg, Germany, ou_persistent22              
5Center of Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN, U.S.A., ou_persistent22              

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Free keywords: Ensemble Refinement with Orientational restraintS (EROS); NMR; residual dipolar coupling (RDC); ubiquitin ensemble
 Abstract: RDCs (residual dipolar couplings) in NMR spectroscopy provide information about protein dynamics complementary to NMR relaxation methods, especially in the previously inaccessible time window between the protein correlation time τc and 50 μs. For ubiquitin, new modes of motion of the protein backbone could be detected using RDC-based techniques. An ensemble of ubiquitin based on these RDC values is found to comprise all different conformations that ubiquitin adopts upon binding to different recognition proteins. These conformations in protein–protein complexes had been derived from 46 X-ray structures. Thus, for ubiquitin recognition by other proteins, conformational selection rather than induced fit seems to be the dominant mechanism.

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Language(s): eng - English
 Dates: 2008-08-012008-01-102008-12-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1042/BST0361433
 Degree: -

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Title: Biochemical Society Transactions
  Other : Biochem Soc Trans
Source Genre: Journal
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Publ. Info: London, UK : Portland Press
Pages: - Volume / Issue: 36 (6) Sequence Number: - Start / End Page: 1433 - 1437 Identifier: ISSN: 0300-5127
CoNE: https://pure.mpg.de/cone/journals/resource/954925507337