Effector binding to liganded hemoglobin (Hb) provides a new understanding of structural
determinants of Hb function. L35, a bezafibrate-related compound, is one of the more potent …

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 has been a long-standing paradigm for understanding protein allostery. Here,
the x-ray structures of two chemically crosslinked, fully liganded hemoglobins, α2β82CA82β …

The highly conserved tryptophan at position β37 occupies a key locus at the hinge region
within the α1β2 interface of the mammalian hemoglobins. This residue is thought to play an …

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 …

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

The crystal structure of human hemoglobin crosslinked between the Lysβ82 residues has
been determined at 2.30 Å resolution. The crosslinking reaction was performed under oxy …

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

Hemoglobin (Hb) is an extensively studied paradigm of proteins that alter their function in
response to allosteric effectors. Models of its action have been used as prototypes for …

Studies of the allosteric mechanism of hemoglobin (Hb) have evolved from
phenomenological descriptions to structure-based molecular mechanisms, as the molecular …