Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …

Hemoglobin (Hb) is a truly remarkable molecule. Human adult hemoglobin (Hb A) has a
tetrameric structure consisting of two α-chains with 141 amino acids each and two β-chains …

Abstract In the protein universe, 30–50% of proteins self-assemble to form symmetrical
complexes consisting of multiple copies of themselves, called homomers. The prevalence of …

A supramolecular protein tetramerization approach has been devised which enables the
controlled formation of a discrete protein tetramer. The supramolecular element cucurbit [8] …

Thermally induced structural transitions of the quaternary structure of the hemoglobin
tetramer (human) in aqueous solution (150 mM ammonium acetate) were investigated using …

Background Human hemoglobin is an allosteric protein that exerts exquisite control over
ligand binding through large-scale conformational changes. The two-state model without …

Allostery in a protein involves effector binding at an allosteric site that changes the structure
and/or dynamics at a distant, functional site. In addition to the chemical equilibrium of ligand …

Allostery in many oligomeric proteins has been postulated to occur via a ligand-binding-
driven conformational transition from the tense (T) to relaxed (R) state, largely on the basis of …

The root mean square deviation (RMSD) and the least RMSD are two widely used similarity
measures in structural bioinformatics. Yet, they stem from global comparisons, possibly …

It is well-known that tetrameric hemoglobin binds ligands cooperatively by undergoing a
ligand-induced T→ R quaternary structure transition, a structure–function relationship that …