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 …

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 …

An atomic model of the sickle hemoglobin (HbS) fiber was synthesized by combining the
molecular coordinates of the fiber (obtained from electron microscopy) with atomic …

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 standard molecular model of the fiber of the sickle hemoglobin (Hbs: β6 Glu→ Val) has
been revised to allow both β6 mutation sites to participate in intermolecular contacts, rather …

Polymerization of sickle hemoglobin (HbS) is the primary pathogenic event of sickle cell
disease. For insight into the nature of the HbS polymer fiber formation, we develop a particle …

An atomic-level understanding of the interactions between hemoglobin molecules that
contribute to the formation of pathological fibers in sickle cell disease remains elusive. By …

By combining X-ray crystallographic co-ordinates of sickle hemoglobin (HbS) molecules with
three-dimensional reconstructions of electron micrographs of HbS fibers we have …

Sickle hemoglobin polymerizes by two types of nucleation: homogeneous nucleation of
aggregates in solution, and heterogeneous nucleation on preexisting polymers. It has been …

We examined the depolymerization of hemoglobin (Hb) S fibers in the presence of CO by
using photolysis of COHbS to create and isolate individual fibers, then removing photolysis …