Protein-Metal Ion Binding Site: Determination with Proton Magnetic Resonance Spectroscopy
- 12 February 1971
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 171 (3971) , 573-574
- https://doi.org/10.1126/science.171.3971.573
Abstract
Proton magnetic resonance spectra of aqueous gelatin were analyzed with respect to composition and molecular interactions. Aqueous gelatin complexes cobaltous ions in the pD range of approximately 3.5 to 7.5. Glutamyl and aspartyl side chains are shown to be the sites of binding.Keywords
This publication has 8 references indexed in Scilit:
- Perturbation of the PMR spectrum of lysozyme by Co+2Biochemical and Biophysical Research Communications, 1969
- 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
- Structural Studies of Ribonuclease. XXIV. The Application of Nuclear Magnetic Resonance Spectroscopy to Distinguish between the Histidine Residues of Ribonuclease1Journal of the American Chemical Society, 1966
- Nuclear Magnetic Resonance of Paramagnetic MoleculesPublished by Elsevier ,1965
- The Nature of the Slowly Exchanging Protons of RibonucleaseJournal of the American Chemical Society, 1962
- AN INTERPRETATION OF THE PROTON MAGNETIC RESONANCE SPECTRUM OF RIBONUCLEASEJournal of the American Chemical Society, 1957
- THE NUCLEAR MAGNETIC RESONANCE SPECTRUM OF RIBONUCLEASE1Journal of the American Chemical Society, 1957