论文信息 - Protein-Metal Ion Binding Site: Determination with Proton Magnetic Resonance Spectroscopy

Protein-Metal Ion Binding Site: Determination with Proton Magnetic Resonance Spectroscopy

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 ∼3.5 to 7.5. Glutamyl and aspartyl side chains are shown to be the sites of binding.

P. Rose

[1] W. D. Phillips,et al. Perturbation of the PMR spectrum of lysozyme by Co+2. , 1969, Biochemical and biophysical research communications.

[2] W. D. Phillips,et al. Proton magnetic resonance spectra of proteins in random-coil configurations. , 1969, Journal of the American Chemical Society.

[3] W. D. Phillips,et al. Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonance. , 1967, Journal of the American Chemical Society.

[4] H. Scheraga,et al. Structural Studies of Ribonuclease. XXIV. The Application of Nuclear Magnetic Resonance Spectroscopy to Distinguish between the Histidine Residues of Ribonuclease1 , 1966 .

[5] M. Saunders,et al. THE NATURE OF THE SLOWLY EXCHANGING PROTONS OF RIBONUCLEASE , 1962 .

[6] J. Vinograd,et al. The Biuret Complex of Gelatin and the Mechanism of Gelation , 1958, Nature.

[7] O. Jardetzky,et al. AN INTERPRETATION OF THE PROTON MAGNETIC RESONANCE SPECTRUM OF RIBONUCLEASE , 1957 .

[8] J. Kirkwood,et al. THE NUCLEAR MAGNETIC RESONANCE SPECTRUM OF RIBONUCLEASE1 , 1957 .