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NMR Applications for Identifying β-TrCP Protein-Ligand Interactions

[ Vol. 11 , Issue. 4 ]


J. Pons, V. Tanchou, J.-P. Girault, G. Bertho and N. Evrard-Todeschi   Pages 283 - 297 ( 15 )


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.


STD-NMR, WaterLOGSY, epitope mapping, docking, phosphorylated peptide, TrCP complex, binding fragment, protein-ligand interactions, magnetization transfer, dissociation constant, ligand competition assays, ATF4, TrCP, HSQC, MBP, NOESY, ROESY, SCF, TOCSY


Universite Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques (UMR 8601 CNRS), 45 rue des Saints-Peres, 75006 Paris, France.

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