The amide nitrogen-15 chemical shift tensors of four peptides determined from carbon-13 dipole-coupled chemical shift powder patterns
- 1 September 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 109 (20) , 5962-5966
- https://doi.org/10.1021/ja00254a011
Abstract
No abstract availableThis publication has 5 references indexed in Scilit:
- 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
- Protein structure by solid state nuclear magnetic resonanceJournal of Molecular Biology, 1985
- High-resolution nitrogen-15 nuclear magnetic resonance studies of .alpha.-lytic protease in solid state. Direct comparison of enzyme structure in solution and solid statesBiochemistry, 1984
- Protein dynamics by solid-state nuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1982
- Acid-base and tautomeric equilibriums in the solid state: nitrogen-15 NMR spectroscopy of histidine and imidazoleJournal of the American Chemical Society, 1982