A refocused and optimized HNCA: Increased sensitivity and resolution in large macromolecules
- 1 March 1992
- journal article
- research article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 2 (2) , 195-202
- https://doi.org/10.1007/bf01875530
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Optimized triple resonance applied to peptides labeled only with 15N. The HN(CO)(CA) experimentJournal of Magnetic Resonance (1969), 1991
- Three-dimensional triple-resonance NMR of 13C/15N-enriched proteins using constant-time evolutionJournal of Magnetic Resonance (1969), 1991
- Observation of labile amide protons via indirect detection of 15N single-quantum transitionsJournal of Magnetic Resonance (1969), 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
- Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteinsJournal 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
- Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteinsJournal of Magnetic Resonance (1969), 1989
- A unified product operator formalism. Application to uniform excitation in heteronuclear correlation 2D NMRJournal of Magnetic Resonance (1969), 1986
- Computer-optimized decoupling scheme for wideband applications and low-level operationJournal of Magnetic Resonance (1969), 1985
- Spin—spin coupling and the conformational states of peptide systemsProgress in Nuclear Magnetic Resonance Spectroscopy, 1976