[13] Solid-State nuclear magnetic resonance structural studies of proteins
- 1 January 1989
- book chapter
- Published by Elsevier
- Vol. 176, 242-275
- https://doi.org/10.1016/0076-6879(89)76015-8
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Solid-state nitrogen-15 NMR of oriented lipid bilayer bound gramicidin A'Biochemistry, 1987
- Determination of the nitrogen-15 and carbon-13 chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patternsJournal of the American Chemical Society, 1987
- The carbonyl carbon-13 chemical shift tensors of five peptides determined from nitrogen-15 dipole-coupled chemical shift powder patternsJournal of the American Chemical Society, 1987
- Measurement of heteronuclear bond distances in polycrystalline solids by solid-state NMR techniquesJournal of the American Chemical Society, 1987
- Protein structure by solid-state NMR spectroscopyQuarterly Reviews of Biophysics, 1987
- Peptide plane orientations determined by fundamental and overtone nitrogen 14 NMRJournal of the American Chemical Society, 1986
- Protein structure by solid state nuclear magnetic resonanceJournal of Molecular Biology, 1985
- Nitrogen-15 spin exchange in a proteinJournal of the American Chemical Society, 1983
- 14N nuclear quadrupole resonance in N‐acetyl amino acidsMagnetic Resonance in Chemistry, 1981
- Two-dimensional 13C NMR of highly oriented polyethyleneThe Journal of Chemical Physics, 1977