Multinuclear and multidimensional NMR methodology for studying individual water molecules bound To peptides and proteins in solution: Principles and applications
- 31 December 1994
- journal article
- review article
- Published by Elsevier in Progress in Nuclear Magnetic Resonance Spectroscopy
- Vol. 26, 171-237
- https://doi.org/10.1016/0079-6565(94)80007-3
Abstract
No abstract availableThis publication has 97 references indexed in Scilit:
- Nuclear Magnetic Resonance Solution Structure of Dendrotoxin K from the Venom of Dendroaspis polylepis polylepisJournal of Molecular Biology, 1993
- Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a Gly-to-Ser mutationBiochemistry, 1993
- Nuclear magnetic resonance detection of bound water molecules in the active site of Lactobacillus casei dihydrofolate reductase in aqueous solutionJournal of Molecular Biology, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Analysis of protein main-chain solvation as a function of secondary structureJournal of Molecular Biology, 1991
- Structure of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- 17O nuclear magnetic resonance studies of some amino acids at natural abundanceMagnetic Resonance in Chemistry, 1980
- Fast kinetics studied by NMRProgress in Nuclear Magnetic Resonance Spectroscopy, 1979
- Molecular orbital theory of the hydrogen bond. 18. Methyl substituent effects on amide hydrogen bondingJournal of the American Chemical Society, 1978
- Molecular motion and structure of aqueous mixtures with nonelectrolytes as studied by nuclear magnetic relaxation methodsThe Journal of Physical Chemistry, 1970