Proton magnetic resonance studies of the tyrosine residues of staphylococcal nuclease using [3,5-2H2]tyrosine
- 25 May 1971
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 236 (2), 468-478
- https://doi.org/10.1016/0005-2795(71)90227-3
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- The isolation of carbon-13 enriched amino acidsBiochimica et Biophysica Acta (BBA) - General Subjects, 1970
- Proton Magnetic Resonance Studies at 220 MHz of the Histidine Residues of Staphylococcal NucleaseNature, 1970
- Nuclear magnetic resonance studies of the structure and binding sites of enzymes: XIV. Inhibitor binding to staphylococcal nucleaseJournal of Molecular Biology, 1970
- Nuclear Magnetic Resonance Spectroscopy of Amino Acids, Peptides, and ProteinsAdvances in protein chemistry, 1970
- Nuclear magnetic resonance studies of the structure and binding sites of enzymesJournal of Molecular Biology, 1969
- Affinity Labeling of the Active Site of Staphylococcal NucleasePublished by Elsevier ,1969
- Proton Magnetic Resonance Studies of Human LysozymeNature, 1969
- Action of staphylococcal nuclease on synthetic substratesBiochemistry, 1969
- The Tyrosyl Residues at the Active Site of Staphylococcal NucleasePublished by Elsevier ,1968
- Staphylococcal Nuclease (Foggi Strain)Published by Elsevier ,1968