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Updated: May 31, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Characterizing weak protein-protein complexes by NMR residual dipolar couplings
Malene Ringkjøbing Jensen1, Jose-Luis Ortega-Roldan, Loïc Salmon
1Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France.
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.
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