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Isotope-Filtered Affinity NMR |
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| Authors: | Nina Gonnella Mengfen Lin Michael J Shapiro James R Wareing Xiaolu Zhang |
| Institution: | aDepartment of Protein Structure, Preclinical Research, Novartis Pharmaceuticals Corporation, 556 Morris Avenue, Summit, New Jersey, 07901;bDepartment of Analytics, Preclinical Research, Novartis Pharmaceuticals Corporation, 556 Morris Avenue, Summit, New Jersey, 07901;cDepartment of Metabolic and Cardiovascular Diseases, Preclinical Research, Novartis Pharmaceuticals Corporation, 556 Morris Avenue, Summit, New Jersey, 07901 |
| 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). |
| Keywords: | Diffusion NMR affinity NMR 13C isotope editing pulse sequence protein binding |
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