Saturation transfer experiments have become useful tools to identify accurately the interaction sites of large biomolecular complexes. Some advantages of the method are reduced protein requirements and no restrictions ont arget size, and no requirement of obtaining high quality protein NMR spectra. The first application was the saturation Transfer difference (STD) scheme ( 99ANG1784) which has been applied in: Recently, an NMR intensity-restrained CORCEMA optimization has been used to refine the conformation of a ligand bound to a receptor protein ( 04JACS8610).
See list of STD NMR Experiments
More Bibliography on STD ... Also see Cross-saturation experiments
