Measurement of HN-H? J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
- 1 November 1994
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 4 (6) , 871-878
- https://doi.org/10.1007/bf00398416
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Enhanced-Sensitivity Triple-Resonance Spectroscopy with Minimal H2O SaturationJournal of Magnetic Resonance, Series A, 1994
- The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurementsJournal of the American Chemical Society, 1993
- Interference between J-couplings and cross-relaxation in solution NMR spectroscopy: consequences for macromolecular structure determinationJournal of the American Chemical Society, 1993
- Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivityJournal of the American Chemical Society, 1992
- Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexibleBiochemistry, 1992
- Precise vicinal coupling constants3JHNα in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experimentsJournal of Biomolecular NMR, 1992
- Accurate measurements of coupling constants from two-dimensional nuclear magnetic resonance spectra of proteins and determination of φ-anglesJournal of Molecular Biology, 1991
- Measurement of NH-C.alpha.H coupling constants in staphylococcal nuclease by two-dimensional NMR and comparison with x-ray crystallographic resultsJournal of the American Chemical Society, 1989
- Accurate measurements of homonuclear HN-H.alpha. coupling constants in polypeptides using heteronuclear 2D NMR experimentsJournal of the American Chemical Society, 1989
- Line narrowing of amide proton resonances in 2D NMR spectra of proteinsJournal of the American Chemical Society, 1989