4D NMR triple-resonance experiments for assignment of protein backbone nuclei using shared constant-time evolution periods
- 15 June 1992
- journal article
- research article
- Published by Elsevier in Journal of Magnetic Resonance (1969)
- Vol. 98 (2) , 443-450
- https://doi.org/10.1016/0022-2364(92)90146-x
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Selective shaped pulse decoupling in NMR: homonuclear [carbon-13]carbonyl decouplingJournal of the American Chemical Society, 1992
- Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteinsJournal of the American Chemical Society, 1992
- Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1991
- Proton, nitrogen-15, and carbon-13 NMR signal assignments of IIIGlc a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniquesBiochemistry, 1991
- Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helixBiochemistry, 1991
- An efficient 3D NMR technique for correlating the proton and15N backbone amide resonances with the α-carbon of the preceding residue in uniformly15N/13C enriched proteinsJournal of Biomolecular NMR, 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
- Enhancement of nuclear magnetic resonance signals by polarization transferJournal of the American Chemical Society, 1979