A new variant of HbS, HbS-Einstein with a deletion of segment α23–26 in the B-helix, has
been assembled by semisynthetic approach. B-helix of the α chain of cis αβ-dimer of HbS …

Abstract Mouse α1–30-horse α31–141 chimeric α-chain, a semisynthetic super-inhibitory α-
chain, inhibits βS-chain dependent polymerization better than both parent α-chains …

Interspecies hybrid HbS (α2Pβ2S), has been assembled in vitro from pig α-globin and
human βS-chain. The α2Pβ2S retains normal tetrameric structure (α2β2) of human Hb and …

Horse α-chain inhibits sickle β-chain-dependent polymerization; however, its inhibitory
potential is not as high as that of mouse α-chain. Horse α-(1–30) and α-(31–141) segments …

The phenotypical severity of sickle cell disease (SCD) can be mitigated by modifying mutant
hemoglobin S (Hb S, Hb α 2 β 2 s) to contain embryonic ζ globin in place of adult α-globin …

Sickle cell disease is caused by the intracellular polymerization of human hemoglobin
containing a mutation of a glutamic acid to a valine residue at the sixth position of the β …

Increasing the affinity of hemoglobin for oxygen represents a feasible and promising
therapeutic approach for sickle cell disease by mitigating the primary pathophysiological …

Hemoglobin is a complex system that undergoes conformational changes in response to
oxygen, allosteric effectors, mutations, and environmental changes. Here, we study allostery …

As part of a comprehensive effort to map the most important regions of sickle hemoglobin
that are involved in polymerization, we have determined whether two sites previously shown …

The identity of intermolecular contact residues in sickle hemoglobin (HbS) fiber is largely
known. However, our knowledge about combinatorial effects of two or more contact sites or …