Heteronuclear NMR Studies of the Molecular Dynamics of Staphylococcal Nuclease
- 1 January 1993
- book chapter
- Published by Springer Nature
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Dynamics of methyl groups in proteins as studied by proton-detected carbon-13 NMR spectroscopy. Application to the leucine residues of staphylococcal nucleaseBiochemistry, 1992
- Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from nitrogen-15 NMR relaxation measurementsBiochemistry, 1992
- Secondary structure and side-chain proton and carbon-13 resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopyBiochemistry, 1991
- 2D heteronuclear NMR measurements of spin-lattice relaxation times in the rotating frame of X nuclei in heteronuclear HX spin systemsJournal of Magnetic Resonance (1969), 1991
- Deletion of the .OMEGA.-loop in the active site of staphylococcal nuclease. II. Effects on protein structure and dynamicsBiochemistry, 1991
- Assignment of the side-chain proton and carbon-13 resonances of interleukin-1.beta. using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopyBiochemistry, 1990
- Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteinsJournal of the American Chemical Society, 1990
- Determination of Three-Dimensional Structures of Proteins and Nucleic Acids in Solution by Nuclear Magnetic Resonance SpectroscopCritical Reviews in Biochemistry and Molecular Biology, 1989
- The Dynamics of ProteinsScientific American, 1986
- A genetic system for analysis of staphylococcal nucleaseGene, 1983