Sickle cell disease is caused by a mutant form of hemoglobin, hemoglobin S, that
polymerizes under hypoxic conditions. The extent and mechanism of polymerization are …

Hemoglobin ζ2β2S is generated by substituting embryonic ζ-globin subunits for the normal α-
globin components of Hb S (α2β2S). This novel hemoglobin has recently been shown to …

The linkage of pair-wise interactions of contact site mutations of HbS has been studied using
Le Lamentin [His-20 (α)→ Gln], Hoshida [Glu-43 (β)→ Gln] and α 2 β 2 T87Q mutations as …

A cluster of amino acid residues located in the AB-GH region of the α-chain are shown in
intra-double strand axial interactions of the hemoglobin S (HbS) polymer. However, αLeu …

The influence of allosteric effectors on the R-state (liganded) conformation of Tg-HbP
(human hemoglobin Presbyterian expressed in transgenic pig) has been probed using a …

Recombinant α-Savaria globin (α S49R) was assembled with β S chains by the alloplex
intermediate pathway to generate tetrameric rHbS-Sarvaria (α 2 S49R β 2 E6V) that …

The influence of the deletion of the tetra peptide segment α23–26 of the B‐helix of the α‐
chain of hemoglobin‐A on its assembly, structure, and functional properties has been …

Organic co‐solvent‐induced secondary conformation of α17–40 of human hemoglobin
facilitates the splicing of E30‐R31 in a mixture of its complementary segments by V8 …

The AB and GH regions of the α-chain are located in spatial proximity and contain a cluster
of intermolecular contact residues of the sickle hemoglobin (HbS) fiber. We have examined …

Protein engineering, generation of mutant or modified forms of protein, has become the first
step for studying the correlation of structure and function of proteins. Design and generation …