In sickle cell anemia, deoxyhemoglobin deforms RBCs by forming fibrils inside that
disintegrate on oxygenation. We studied 100 ns long all-atom molecular dynamics (MD) for …

Sickle cell disease is a hemoglobinopathy resulting from a point mutation from glutamate to
valine at position six of the β‐globin chains of hemoglobin. This mutation gives rise to …

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 …

Abstract Hemoglobin (Hb), an oxygen‐binding protein composed of four subunits (α1, α2,
β1, and β2), is a well‐known example of allosteric proteins that are capable of cooperative …

Sickle cell disease is caused by the amino acid substitution of glutamic acid to valine, which
leads to the polymerization of deoxygenated sickle hemoglobin (HbS) into long strands …

Protein aggregation is associated with various diseases, including Alzheimer and Parkinson
as well as sickle cell disease (SCD). From a molecular point of view, protein aggregation …

Sickle cell anemia reflects a single change in the amino acid building blocks of the oxygen-
transport protein, hemoglobin. The beta subunits have the neutral hydrophobic amino acid …

Human hemoglobin (HbA) is one of the prototypal systems used to investigate structure–
function relationships in proteins. Indeed, HbA has been used to develop the basic concepts …

Hemoglobin exhibits allosteric structural changes upon ligand binding due to the dynamic
interactions between the ligand binding sites, the amino acids residues and some other …

Molecular dynamics simulations have been used to investigate the thermodynamic stability
of axial contacts in sickle-cell hemoglobin (HbS). Free energy changes were evaluated for …