Conformational and functional properties of hemoglobin in perturbed solvent: Kinetics of O2 release
- 1 July 1983
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 22 (7) , 1677-1696
- https://doi.org/10.1002/bip.360220706
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Linked functions in allosteric proteinsJournal of Molecular Biology, 1981
- Spin equilibrium and quaternary structure change in hemoglobin A. Experiments on a quantitative probe of the stereochemical mechanism of hemoglobin cooperativityBiochemistry, 1979
- Estimation of parameters in a multi-affinity-state model for haemoglobin from oxygen binding data in whole blood and in concentrated haemoglobin solutionsJournal of Molecular Biology, 1978
- Temperature induced difference spectra of Oxy and Deoxy hemoglobin in the near IR, visible and soret regionsBiochemical and Biophysical Research Communications, 1977
- Phosphate-dependent spectroscopic changes in liganded hemoglobinBiochemical and Biophysical Research Communications, 1974
- Influence of globin structure on the state of the heme. I. Human deoxyhemoglobinBiochemistry, 1974
- An allosteric model of hemoglobin: I, kineticsJournal of Molecular Biology, 1971
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- The determination of the individual equilibrium constants of the four intermediate reactions between oxygen and sheep haemoglobinProceedings of the Royal Society of London. B. Biological Sciences, 1955
- DIELECTRIC CONSTANTS OF SOME ORGANIC SOLVENT-WATER MIXTURES AT VARIOUS TEMPERATURESJournal of the American Chemical Society, 1932