1. Characterizing weak protein–protein complexes by NMR residual dipolar couplings
- Author
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Martin Blackledge, Malene Ringkjøbing Jensen, Loïc Salmon, Jose-Luis Ortega-Roldan, and Nico A. J. van Nuland
- Subjects
Quantitative Biology::Biomolecules ,Magnetic Resonance Spectroscopy ,Macromolecular Substances ,Chemistry ,Quantitative Biology::Molecular Networks ,Biophysics ,Proteins ,General Medicine ,Nuclear magnetic resonance spectroscopy ,Molecular Dynamics Simulation ,Resonance (chemistry) ,Affinities ,SH3 domain ,Protein Structure, Tertiary ,Protein–protein interaction ,Quantitative Biology::Subcellular Processes ,Dissociation constant ,Molecular dynamics ,Protein structure ,Computational chemistry ,Protein Binding - 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.
- Published
- 2011
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