Optimization of Three-Dimensional TROSY-Type HCCH NMR Correlation of Aromatic 1H–13C Groups in Proteins
- 31 August 1999
- journal article
- editorial
- Published by Elsevier in Journal of Magnetic Resonance
- Vol. 139 (2) , 447-450
- https://doi.org/10.1006/jmre.1999.1796
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Spin-State-Selective TPPI: A New Method for Suppression of Heteronuclear Coupling Constants in Multidimensional NMR ExperimentsJournal of Magnetic Resonance, 1999
- Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in 13C-Labeled ProteinsJournal of the American Chemical Society, 1998
- Attenuated T 2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solutionProceedings of the National Academy of Sciences, 1997
- The solution structure of the N-terminal domain of α2-macroglobulin receptor-associated proteinProceedings of the National Academy of Sciences, 1997
- Spin-state-selective coherence transfer via intermediate states of two-spin coherence in IS spin systems: Application to E.COSY-type measurement of J coupling constantsJournal of Biomolecular NMR, 1997
- Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivityJournal of the American Chemical Society, 1992
- Reduction of multiplet complexity in COSY-type NMR spectraMolecular Physics, 1991