title: NMR applications for identifying β-TrCP protein-ligand interactions.
abstract: In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.
authors.affiliation: Université Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques (UMR 8601 CNRS), 45 rue des Saint-Pères, 75006 Paris, France.
authors.forename: J
authors.initials: J
authors.lastname: Pons
authors.forename: V
authors.initials: V
authors.lastname: Tanchou
authors.forename: J-P
authors.initials: JP
authors.lastname: Girault
authors.forename: G
authors.initials: G
authors.lastname: Bertho
authors.forename: N
authors.initials: N
authors.lastname: Evrard-Todeschi
mesh_terms: D003198:Computer Simulation; D006801:Humans; D008024:Ligands; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D044844:beta-Transducin Repeat-Containing Proteins / Q000737:chemistry*
chemical_list: D008024:Ligands; D044844:beta-Transducin Repeat-Containing Proteins