Haemoglobin: The surface buried between the α1β1 and α2β2 dimers in the deoxy and oxy structures
- 1 May 1985
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 183 (2), 267-270
- https://doi.org/10.1016/0022-2836(85)90219-0
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Solvent effects on allosteric equilibria: stabilization of T and R conformations of Escherichia coli aspartate transcarbamylase by organic solventsBiochemistry, 1984
- The crystal structure of human deoxyhaemoglobin at 1.74 Å resolutionJournal of Molecular Biology, 1984
- Effect of some organic cosolvents on the reaction of hemoglobin with oxygenBiopolymers, 1981
- Energetics of subunit assembly and ligand binding in human hemoglobinBiophysical Journal, 1980
- Effect of some monohydric alcohols on the oxygen affinity of hemoglobin: Relevance of solvent dielectric constant and hydrophobicityBiopolymers, 1979
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- The structure of horse methaemoglobin at 2.0 Å resolutionJournal of Molecular Biology, 1977
- Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2·5 Å resolution: Refinement of the atomic modelJournal of Molecular Biology, 1975
- Hydrophobic bonding and accessible surface area in proteinsNature, 1974
- The interpretation of protein structures: Estimation of static accessibilityJournal of Molecular Biology, 1971