Conformational changes in the hemoglobin S system as seen by proton binding.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Conformational relevance of the beta6Glu replaced by Val mutation in the beta subunits and in the beta(1-55) and beta(1-30) peptides of hemoglobin S.
2. Effect of the beta6 Glu replaced by Val mutation on the optical activity of hemoglobin S and of its beta subunits.
3. A decreased effect of organic phosphates on hemoglobin S at low concentrations
4. Abnormal Precipitation of Oxyhemoglobin S by Mechanical Shaking
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1. Inhibition of Hemoglobin S Polymerization in Vitro by a Novel 15-mer EF-Helix β73 Histidine-Containing Peptide;Biochemistry;2006-06-14
2. Sickle hemoglobin is more fusogenic than normal hemoglobin at physiological pH and ionic strength conditions;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;1998-03
3. Effects of β6 amino acid hydrophobicity on stability and solubility of hemoglobin tetramers;FEBS Letters;1993-01-02
4. Dependence on pH of formation and oxygen affinity of hemoglobin S fibers in the presence and absence of phosphates and polyphosphates;Biophysical Chemistry;1987-12
5. Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions.;Journal of Biological Chemistry;1984-09
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