1H Nuclear magnetic resonance spectroscopy of yeast copper-zinc superoxide dismutase. Structural homology with the bovine enzyme
- 1 November 1978
- journal article
- research article
- Published by Springer Nature in Carlsberg Research Communications
- Vol. 43 (6) , 439-449
- https://doi.org/10.1007/bf02906114
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Competitive inhibition of Cu, Zn superoxide dismutase by monovalent anionsBiochemical and Biophysical Research Communications, 1977
- Investigation of the structure of bovine erythrocyte superoxide dismutase by proton nuclear magnetic resonance spectroscopyBiochemistry, 1977
- Evidence for a coordination position available to solute molecules on one of the metals at the active center of reduced bovine superoxide dismutaseBiochemical and Biophysical Research Communications, 1976
- Studies of the histidine residues of triose phosphate isomerase by proton magnetic resonance and x-ray crystallographyJournal of Molecular Biology, 1976
- Pulse methods for the simplification of protein NMR spectraFEBS Letters, 1975
- Superoxide DismutasesAnnual Review of Biochemistry, 1975
- Observation of histidine residues in proteins by nuclear magnetic resonance spectroscopyAccounts of Chemical Research, 1975
- Simplification of the Proton Magnetic Resonance Spectrum of Ribonuclease by Difference SpectroscopyNature, 1971
- Proton magnetic resonance spectra of proteins in random-coil configurationsJournal of the American Chemical Society, 1969
- Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonanceJournal of the American Chemical Society, 1967