Significant reduction in oxygen affinity resulting from interactions between heterotropic
allosteric effectors and hemoglobin in not only the unligated derivative but also the fully …

Careful analyses of precise oxygenation curves of hemoglobin (Hb) clearly indicate that,
contrary to the common belief, allosteric effectors exert a dramatic control of the oxygenation …

By introducing an additional H-bond in the α1β2 subunit interface or altering the charge
properties of the amino acid residues in the α1β1 subunit interface of the hemoglobin …

Abstract Analysis of the tertiary structural alterations in hemoglobin induced by ligand
binding demonstrates that an allosteric core composed of the heme, histidine F8, the FG …

Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo
quaternary structural transitions in response to concentration changes of a specific ligand …

A longstanding challenge in macromolecular biochemistry has been the question of how the
four “active site” hemes of human hemoglobin (Hb) interact cooperatively over widely …

The contribution of heterotropic effectors to hemoglobin allostery is still not completely
understood. With the recently proposed global allostery model, this question acquires crucial …

Hemoglobin (Hb) remains the most studied and understood example of an allosteric protein.
It exists in equilibrium between a tense or T state (unliganded or deoxygenated Hb) and 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 …

The two-state allosteric model of Monod, Wyman, and Changeux (MWC) provides an
excellent description of homotropic effects in a vast array of equilibrium and kinetic …