Journal article

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

Lange O, Lakomek N, Fares C, Schroder G, Walter K, Becker S, Meiler J, Grubmuller H, Griesinger C, de Groot B ...see all

Science, vol. 320, issue 5882 (2008) pp. 1471-1475

  • 494


    Mendeley users who have this article in their library.
  • 670


    Citations of this article.
Sign in to save reference


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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text


  • O. F. Lange

  • N.-A. Lakomek

  • C. Fares

  • G. F. Schroder

  • K. F. A. Walter

  • S. Becker

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free