EXPERIMENTAL NMR TECHNIQUES FOR STUDIES OF PROTEIN LIGAND INTERACTIONS

NMR studies of protein-ligand interactions range from using NMR as a t ool with which to monitor ligand binding to the determination of the t hree-dimensional structure of complexes at atomic resolution. In recen t years, selective and uniform enrichment with stable isotopes has pro moted the investigation of ever larger systems at increasing resolutio n, and significant advances have been made using NMR techniques that f ocus specifically on the interaction of proteins and ligands.