title: Characterizing weak protein-protein complexes by NMR residual dipolar couplings.
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.
authors.affiliation: Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France.
authors.forename: Malene Ringkjøbing
authors.initials: MR
authors.lastname: Jensen
authors.forename: Jose-Luis
authors.initials: JL
authors.lastname: Ortega-Roldan
authors.forename: Loïc
authors.initials: L
authors.lastname: Salmon
authors.forename: Nico
authors.initials: N
authors.lastname: van Nuland
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
mesh_terms: D046911:Macromolecular Substances / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation* / Q000379:methods; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000502:physiology*; D011506:Proteins / Q000737:chemistry*
chemical_list: D046911:Macromolecular Substances; D011506:Proteins