Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution.
An improved version of the three-dimensional HCCH-COSY NMR experiment is described that correlates the resonances of geminal and vicinal proton pairs with the chemical shift of the 13C nucleus attached to one of the protons. The experiment uses constant-time evolution of transverse 13C magnetization which optimizes transfer of magnetization and thus improves the sensitivity of the experiment over the original scheme. The experiment is demonstrated for calmodulin complexed with a 26-residue peptide comprising the binding site of skeletal muscle myosin light chain kinase.
Ikura
M
M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Kay
L E
LE
Bax
A
A
D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism; D002247:Carbon Isotopes; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D009219:Myosin-Light-Chain Kinase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D011817:Rabbits; D014316:Tritium
D002147:Calmodulin; D002247:Carbon Isotopes; D011506:Proteins; D014316:Tritium; D009219:Myosin-Light-Chain Kinase