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- W2017146178 abstract "Homo- and heterotetramer formations of β112 variants (β112Cys→Asp, β112Cys→Ser, β112Cys→Thr, and β112Cys→Val) of hemoglobin were characterized in the presence and absence of β16Gly→Aspin vitro. In all cases an alteration in overall surface charge (β16Gly→Asp) decreased the β4 homotetramer stability (association constants as determined by gel-permeation chromatography) albeit to differing extents. In contrast, competition experiments of hemoglobin subunits showed that heterotetramer formation was promoted by this substitution. Order of increase in tetramer formation by the additional negative surface charge in the β112 variants was as follows: Hb βG16D, C112D > Hb βG16D, C112S > Hb βG16D > Hb G16D, C112T > Hb βG16D, C112V. Thus, the overall surface charge of the β chain and its contribution to electrostatic interaction in these instances appear to act in synergy with α1β1 interface residues to affect the assembly of hemoglobin molecules." @default.
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- W2017146178 date "2000-04-01" @default.
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- W2017146178 title "Surface and Interface β-Chain Residues Synergistically Affect Hemoglobin Assembly" @default.
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- W2017146178 doi "https://doi.org/10.1006/bbrc.2000.2504" @default.
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