Structure-function relationships in the low-affinity mutant haemoglobin aalborg (Gly74 (E18)β → Arg)
- 1 August 1992
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 226 (3) , 883-888
- https://doi.org/10.1016/0022-2836(92)90638-z
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobinsJournal of Molecular Biology, 1990
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- Binding of diphosphoglycerate and ATP to oxyhemoglobin dimersJournal of Molecular Biology, 1986
- Haemoglobin: The surface buried between the α1β1 and α2β2 dimers in the deoxy and oxy structuresJournal of Molecular Biology, 1985
- Stereochemically restrained refinement of macromolecular structuresPublished by Elsevier ,1985
- Bonding of molecular oxygen to T state human haemoglobinNature, 1984
- [25] Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatusPublished by Elsevier ,1981
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Structure and function of haemoglobinProgress in Biophysics and Molecular Biology, 1976
- X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human DeoxyhaemoglobinNature, 1972