The effect of quaternary structure on the state of the α and β subunits within nitrosyl haemoglobin
- 1 January 1978
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 532 (1) , 17-28
- https://doi.org/10.1016/0005-2795(78)90443-9
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- The Effect of Inositol Hexaphosphate on the Absorption Spectra of α and β Chains in Nitrosyl HemoglobinThe Journal of Biochemistry, 1976
- Influence of globin structures on the state of the heme. IV. Ferrous low spin derivativesBiochemistry, 1976
- Correlation between quaternary structure and ligand dissociation kinetics for fully liganded hemoglobinBiochemistry, 1975
- Low temperature photodissociation of hemoproteins: Carbon monoxide complex of myoglobin and hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1974
- Influence of globin structure on the state of the heme. I. Human deoxyhemoglobinBiochemistry, 1974
- Influence of globin structure on the state of the heme. III. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interactionBiochemistry, 1974
- Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobinBiochemistry, 1974
- On the influence of allosteric effectors on the electron paramagnetic spectrum of nitric oxide hemoglobinFEBS Letters, 1972
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965