Sensitivity Enhancement of Triple-Resonance Protein NMR Spectra by Proton Evolution of Multiple-Quantum Coherences Using a Simultaneous 1H and 13C Constant-Time Evolution Period
- 1 October 1997
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 119 (39) , 9274-9278
- https://doi.org/10.1021/ja970734k
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Assignment of Side-Chain 13C Resonances in Perdeuterated ProteinsJournal of the American Chemical Society, 1995
- An HCCNH Triple-Resonance Experiment Using Carbon-13 Isotropic Mixing for Correlating Backbone Amide and Side-Chain Aliphatic Resonances in Isotopically Enriched ProteinsJournal of Magnetic Resonance, Series B, 1993
- A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experimentsJournal of Biomolecular NMR, 1993
- Carbon-hydrogen insertions in the reactions of Fischer carbene complexes with ketene acetalsJournal of the American Chemical Society, 1992
- Improved 4D NMR experiments for the assignment of backbone nuclei in13C/15N labelled proteinsJournal of Biomolecular NMR, 1992
- Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteinsJournal of the American Chemical Society, 1992
- Structures of Larger Proteins in Solution: Three- and Four-Dimensional Heteronuclear NMR SpectroscopyScience, 1991
- A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulinBiochemistry, 1990
- Hyperconjugative distortions and the cyclopentyl cation structureJournal of the American Chemical Society, 1989
- Enhancement of nuclear magnetic resonance signals by polarization transferJournal of the American Chemical Society, 1979