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 tau(c) and 50 micros. 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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Lakomek NA,Lange OF,Walter KF,Farès C,Egger D,Lunkenheimer P,Meiler J,Grubmüller H,Becker S,de Groot BL,Griesinger Cdoi
10.1042/BST0361433subject
Has Abstractpub_date
2008-12-01 00:00:00pages
1433-7issue
Pt 6eissn
0300-5127issn
1470-8752pii
BST0361433journal_volume
36pub_type
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