title: 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 using 13C isotope editing and PFG diffusion-edited NMR. This new experiment is demonstrated using 13C/15N-labeled stromelysin catalytic domain (SCD). Copyright 1998 Academic Press.
authors.affiliation: Preclinical Research, Novartis Pharmaceuticals Corporation, 556 Morris Avenue, Summit, New Jersey, 07901
authors.initials: N
authors.lastname: Gonnella
authors.initials: M
authors.lastname: Lin
authors.initials: MJ
authors.lastname: Shapiro
authors.initials: JR
authors.lastname: Wareing
authors.initials: X
authors.lastname: Zhang