Allosteric properties of haemoglobin β41 (C7) Pheå Tyr: a stable, low-oxygen-affinity variant synthesized in Escherichia coli
- 23 September 1992
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1159 (2) , 223-226
- https://doi.org/10.1016/0167-4838(92)90029-d
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Steric and hydrophobic determinants of the solubilities of recombinant sickle cell hemoglobinsProtein Science, 1992
- Site-directed mutagenesis in haemoglobin: Functional role of tyrosine-42(C7)α at the α1-β2 interfaceJournal of Molecular Biology, 1991
- Functional role of the distal valine (E11) residue of α subunits in human haemoglobinJournal of Molecular Biology, 1991
- NMR study of Human Mutant Hemoglobins Synthesized in Escherichia coliPublished by Elsevier ,1989
- T-state hemoglobin with four ligands boundBiochemistry, 1988
- Generation of β-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coliNature, 1984
- Hemoglobin M equon beta 41 (C7) phenylalanine leads to tyrosineBlood, 1976
- Extinction coefficients for use in equations for the spectrophotometric analysis of haemoglobin mixturesAnalytical Biochemistry, 1975
- 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