The mutated hemoglobin HbC (β6 Glu→ Lys), in the oxygenated (R) liganded state, forms
crystals inside red blood cells of patients with CC and SC diseases. Static and dynamic light …

Recent molecular dynamics (MD) simulations of human hemoglobin (Hb) give results in
disagreement with experiment. Although it is known that the unliganded (T 0) and liganded …

Hemoglobin is the prototypic allosteric protein. Still, its molecular allosteric mechanism is not
fully understood. To elucidate the mechanism of cooperativity on an atomistic level, we …

Prompted by the reported lack of solvation effects on the oxygen affinity of fish (trout I)
hemoglobin that questioned allosteric water binding in human hemoglobin A (Bellelli, A …

Sickle cell hemoglobin (HbS) is a mutant, whose polymerization while in deoxy state in the
venous circulation underlies the debilitating sickle cell anemia. It has been suggested that …

Based on the detailed atomic structure of the intermolecular contact sites in the
deoxyhemoglobin S crystal, we are developing peptides as stereospecific inhibitors of the …

We perform a computer simulation of the quaternary structure change during the allosteric
transition of hemoglobin. The simulation is based on a docking procedure by which αβ …

The pathology of sickle cell disease is caused by polymerization of the abnormal
hemoglobin S upon deoxygenation in the tissues to form fibers in red cells, causing them to …

The interface between hemoglobin (Hb) and its environment, in particular water, is of great
physiological relevance. Here, results from in vitro, in vivo, and computational experiments …