Transferred-NOE experiments ( 94PROG517) provide conformational information of bound ligands from intra-ligand NOE data in weakly-binding rapid exchange ligand/protein complexes and also to locate the corresponding binding sites. When a small molecule binds a large molecule suchas a protein, the numerical sign and magnitudes of the NOEs change. Several examples include: The accuracy of the peptide-protein structures obtained from transferred-NOE data has been studied and simulated ( 00JB17-17) and the effect of intermolecular relaxation evaluated ( 02JB303-22) .This method have been also used for screening purposes of mixtures of small, biologically-active molecules in the presence of large molecules, like proteins ( 97EJB705-246, 99ANG98, and 00JMC2093).
Variants of the NOESY pulse sequence to minimize undesired ZQC have been proposed ( 00MRC315).