1H nuclear magnetic resonance study of the histidine residues of insulin
- 1 August 1981
- journal article
- letter
- Published by Elsevier in Journal of Molecular Biology
- Vol. 150 (4) , 609-613
- https://doi.org/10.1016/0022-2836(81)90385-5
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solutionBiochemistry, 1980
- Hydrogen–deuterium exchange of the C-2 protons of histidine and histidine peptides and proteinsJournal of the Chemical Society, Perkin Transactions 2, 1980
- Conformational analysis by nuclear magnetic resonance: insulinBiochemistry, 1979
- Structure and biological activity of hagfish insulinJournal of Molecular Biology, 1979
- Synthesis and Biological Activity of Seventeen Analogues of Human InsulinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Nuclear‐Magnetic‐Resonance Study of the Histidine Residues of S‐Peptide and S‐Protein and Kinetics of 1H‐2H Exchange of Ribonuclease AEuropean Journal of Biochemistry, 1977
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- A study of the histidine residues of human carbonic anhydrase C using 270 MHz proton magnetic resonanceJournal of Molecular Biology, 1975
- A study of the histidine residues of human carbonic anhydrase B using 270 MHz proton magnetic resonanceJournal of Molecular Biology, 1974
- Proton Magnetic Resonance Studies of Metal Complexes of Imidazole, Purine, and Pyrimidine Derivatives1Journal of the American Chemical Society, 1966