Studies of protein hydration in aqueous solution by high-resolution nuclear magnetic resonance spectroscopy
- 5 June 1992
- journal article
- research article
- Published by Wiley in International Journal of Quantum Chemistry
- Vol. 42 (5) , 1553-1561
- https://doi.org/10.1002/qua.560420528
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Structure of form III crystals of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1987
- Protein structures in solution by nuclear magnetic resonance and distance geometryJournal of Molecular Biology, 1987
- Structure of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambinProceedings of the National Academy of Sciences, 1984
- Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solutionJournal of Molecular Biology, 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Studies of J-connectivities and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experimentsBiochemical and Biophysical Research Communications, 1980
- Cross relaxation and spin diffusion effects on the proton NMR of biopolymers in H2OFEBS Letters, 1978
- Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolutionActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1975
- Pulsed Fourier-Transform NMR Spectrometer for Use with H2O SolutionsThe Journal of Chemical Physics, 1971