Résumé
Nuclear magnetic resonance (NMR) is a powerful technique for probing and characterizing protein–ligand interactions. The technique includes both ligand‐observed and protein‐observed NMR experiments for ligand screening, measurement of protein–ligand affinity, and assessment of the binding modes of the ligands. The ligand‐observed methods discussed here are NOE‐based approaches, namely, the saturation transfer difference, WaterLOGSY, and transferred NOESY, including the INPHARMA experiments that have been less used so far. Protein‐observed experiments discussed here involve the use of chemical shift perturbations observed on protein NMR spectra upon ligand binding. We examine how these chemicals shift perturbations can be used for the analysis of protein–ligand complexes, including fast structure determination when combined with docking.