European Biophysics Journal

, Volume 40, Issue 12, pp 1371–1381 | Cite as

Characterizing weak protein–protein complexes by NMR residual dipolar couplings

  • Malene Ringkjøbing Jensen
  • Jose-Luis Ortega-Roldan
  • Loïc Salmon
  • Nico van Nuland
  • Martin Blackledge
Original Paper

Abstract

Protein–protein interactions occur with a wide range of affinities from tight complexes characterized by femtomolar dissociation constants to weak, and more transient, complexes of millimolar affinity. Many of the weak and transiently formed protein–protein complexes have escaped characterization due to the difficulties in obtaining experimental parameters that report on the complexes alone without contributions from the unbound, free proteins. Here, we review recent developments for characterizing the structures of weak protein–protein complexes using nuclear magnetic resonance spectroscopy with special emphasis on the utility of residual dipolar couplings.

Keywords

NMR Interaction Protein Dynamics Structure Complex 

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Copyright information

© European Biophysical Societies' Association 2011

Authors and Affiliations

  • Malene Ringkjøbing Jensen
    • 1
  • Jose-Luis Ortega-Roldan
    • 2
  • Loïc Salmon
    • 1
  • Nico van Nuland
    • 3
  • Martin Blackledge
    • 1
  1. 1.Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre EbelCEA-CNRS-UJF UMR 5075GrenobleFrance
  2. 2.Department of BiochemistryUniversity of OxfordOxfordUK
  3. 3.Structural Biology Brussels, VIB Department of Molecular and Cellular InteractionsVrije Universiteit BrusselBrusselBelgium

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