Proteins that function in aqueous solution can be perturbed by the solvent. Here we present
experimental studies on two such interactions in the hemoglobin molecule.(1) Hemoglobin's …

Under physiological conditions, sickle hemoglobin, a natural mutant of human hemoglobin A
with a surface hydrophobic valine in place of a negatively charged glutamic acid …

We have studied the self-assembly of Hemoglobin C-Harlem (HbC-Harlem), a double
mutant of hemoglobin that possesses the β6 Glu→ Val mutation of sickle hemoglobin (HbS) …

The solubility equilibrium between monomer and polymer which has been shown to exist in
deoxyhemoglobin S solutions is examined in solutions partially saturated with carbon …

Sickle hemoglobin (HbS) polymerization occurs when the concentration of deoxyHbS
exceeds a well-defined solubility. In experiments using sickle hemoglobin droplets …

Understanding the physical basis of protein aggregation covers strong physical and
biomedical interests. Sickle hemoglobin (HbS) is a point‐mutant form of normal human adult …

Sickle cell disease is a genetic disorder associated with a single mutation (Glu-β6→ Val-β6)
in the β chains of hemoglobin, causing the polymerization of deoxygenated sickle cell …

It has long been known that a simple hard particle model quantitatively explains the osmotic
properties of monomeric hemoglobin near its isoelectric point. However, we find that a hard …

We have measured the solubility, and the rates of homogeneous and heterogeneous
nucleation on sickle hemoglobin (HbSβ6 Glu→ Val) additionally modified by site-directed …

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