Proton Magnetic Resonance Studies at 220 MHz of the Histidine Residues of Staphylococcal Nuclease
- 1 November 1970
- journal article
- Published by Springer Nature in Nature
- Vol. 228 (5272), 642-644
- https://doi.org/10.1038/228642a0
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- On-line computer-assisted analysis of 220 MHz NMR data of protein imidazole resonancesBiochemical and Biophysical Research Communications, 1970
- Nonlinear Regression With Linear Constraints: An Extension of the Magnified Diagonal MethodJournal of the ACM, 1970
- Nuclear magnetic resonance studies of the structure and binding sites of enzymes: XIV. Inhibitor binding to staphylococcal nucleaseJournal of Molecular Biology, 1970
- Kinetics of Folding of Staphylococcal NucleaseScience, 1970
- Nuclear magnetic resonance studies of the structure and binding sites of enzymes: VIII. Inhibitor binding to ribonucleaseJournal of Molecular Biology, 1969
- Proton Magnetic Resonance Studies of Human LysozymeNature, 1969
- NMR‐Studies on the Structure of the Active Site of Pancreatic Ribonuclease AEuropean Journal of Biochemistry, 1969
- Nuclear magnetic resonance studies of the structure and binding sites of enzymes. VII. Solvent and temperature effects on the ionization of histidine residues of ribonucleaseBiochemistry, 1969
- Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonanceJournal of the American Chemical Society, 1967
- A Nuclear Magnetic Resonance Study of Structures of Cobalt(II)-Histidine ComplexesJournal of the American Chemical Society, 1963