Isotope-Filtered Affinity NMR

Abstract

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 using13C isotope editing and PFG diffusion-edited NMR. This new experiment is demonstrated using13C/15N-labeled stromelysin catalytic domain (SCD).