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.

Keywords: 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