Isotope-filtered affinity NMR

A double-editing pulse sequence has been developed that allows the direct observation of protein binding ligand(s) from a mixture of compounds. This technique should aid the discovery of lead pharmaceutical compounds. The proton NMR signals from protein and the nonbinding ligands are simultaneously eliminated using C-13 isotope editing and PFG diffusion-edited NMR. This new experiment is demonstrated using C-13/N-15-labeled stromelysin catalytic domain (SCD). (C) 1998 Academic Press.