Improved 4D NMR experiments for the assignment of backbone nuclei in13C/15N labelled proteins
- 1 November 1992
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 2 (6) , 631-637
- https://doi.org/10.1007/bf02192851
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- 4D NMR triple-resonance experiments for assignment of protein backbone nuclei using shared constant-time evolution periodsJournal of Magnetic Resonance (1969), 1992
- Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradientsJournal of Magnetic Resonance (1969), 1992
- A 3D triple-resonance NMR technique for qualitative measurement of carbonyl-Hβ J couplings in isotopically enriched proteinsJournal of Magnetic Resonance (1969), 1992
- Three-dimensional triple-resonance NMR of 13C/15N-enriched proteins using constant-time evolutionJournal of Magnetic Resonance (1969), 1991
- The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteinsJournal of Magnetic Resonance (1969), 1991
- Comparison of techniques for 1H-detected heteronuclear 1H15N SpectroscopyJournal of Magnetic Resonance (1969), 1990
- Conformation-independent sequential NMR connections in isotope-enriched polypeptides by 1H13C15N triple-resonance experimentsJournal of Magnetic Resonance (1969), 1990
- Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteinsJournal of Magnetic Resonance (1969), 1990
- Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H2O solutionsJournal of Magnetic Resonance (1969), 1989
- Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteinsJournal of Magnetic Resonance (1969), 1989