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

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 Trans

authors

Lakomek NA,Lange OF,Walter KF,Farès C,Egger D,Lunkenheimer P,Meiler J,Grubmüller H,Becker S,de Groot BL,Griesinger C

doi

10.1042/BST0361433

subject

Has Abstract

pub_date

2008-12-01 00:00:00

pages

1433-7

issue

Pt 6

eissn

0300-5127

issn

1470-8752

pii

BST0361433

journal_volume

36

pub_type

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