The molecular mechanism of the temperature enhancement of proton magnetic relaxation rates in methaemoprotein solutions
- 1 December 1974
- journal article
- Published by Elsevier in Biophysical Chemistry
- Vol. 2 (4), 359-368
- https://doi.org/10.1016/0301-4622(74)80063-3
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- A proton magnetic relaxation study of ferrimyoglobin in aqueous ionic solutionsBiophysical Chemistry, 1973
- A proton magnetic relaxation study of human ferrihaemoglobin in aqueous salt solutionsBiopolymers, 1973
- Possible Structural and Functional Differences of the Two Conformers of Myoglobin-like Molecules with Respect to the Haem-Haem InteractionNature, 1971
- Haem hydration and displacement in the pre-denaturational conformational transition of the myoglobin moleculeBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Factors influencing the absorption spectrum of vertebrate hemoglobin in solutionBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- Solvent perturbation studies of heme proteins and other colored proteinsArchives of Biochemistry and Biophysics, 1969
- Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic ModelNature, 1968
- Dissociation of Human CO-Hemoglobin by Urea, Guanidine Hydrochloride, and Other Reagents*Biochemistry, 1965
- Standardization of hemoglobinometryClinica Chimica Acta; International Journal of Clinical Chemistry, 1960
- Magnetic Studies of Ferrihemoglobin Reactions. II. Equilibria and Compounds with Azide Ion, Ammonia, and Ethanol1Journal of the American Chemical Society, 1940