Hemoglobin A2 (α2δ2) is an important hemoglobin variant which is a minor component (2−
3%) in the circulating red blood cells, and its elevated concentration in β-thalassemia is a …

The ability of hemoglobin (Hb) to transport respiratory gases is directly linked to its
quaternary structure properties and reversible changes between T (tense) and R (relax) …

X-ray crystallography has played a key role in understanding the relationship between
protein structure and physiological function. In particular, X-ray analysis of hemoglobin (Hb) …

We compare the role of a conformational switch and that of a point mutation in the
thermodynamic stability of a protein solution and in the consequent propensity toward …

Hemoglobin was one of the first protein structures to be determined by X-ray crystallography
and served as a basis for the two-state MWC model for the mechanism of allosteric proteins …

The α-globin of human hemoglobin was expressed in Escherichia coli and was refolded with
heme in the presence and in the absence of native β-chains. The functional and structural …

We present molecular dynamics simulations of unliganded human hemoglobin (Hb) A under
physiological conditions, starting from the R, R2, and T state. The simulations were carried …

A minor hemoglobin component of human red cell hemolysate, HbA1c, is the result of the
non-enzymatic reaction of glucose with the α-amino groups of the valine residues at the N …

The α-hemoglobin-stabilizing protein (AHSP), a small protein of 102 amino acids, is
synthesized in red blood cell precursors. It binds specifically to α-hemoglobin (α-Hb) …

Initial crystallographic studies suggested that fully liganded mammalian hemoglobin can
adopt only a single quaternary structure, the quaternary R structure. However, more recent …