Conspectus Sickle cell disease (SCD) is an inherited blood disorder caused by a point
mutation in hemoglobin (Hb), the protein in the red blood cell (RBC) responsible for the …

Background Human hemoglobin is an allosteric protein that equilibrates between the deoxy
or tense (T) state and the oxy or relaxed (R) state. Arrangement of the four subunits around a …

The rational design and X-ray crystallographic analyses of two symmetrical allosteric
effectors of hemoglobin (Hb) are reported. Compound design was directed by the previously …

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 …

Hemoglobin (Hb) modifiers that stereospecifically inhibit sickle hemoglobin polymer
formation and/or allosterically increase Hb affinity for oxygen have been shown to prevent …

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

Revised Manuscript Received June 27, 1995® abstract: Monoaldehyde allosteric effectors
of hemoglobin were designed, using molecular modeling software (GRID), to form a Schiff …

The crystal structure of human deoxy hemoglobin (Hb) complexed with a potent allosteric
effector (2‐[4‐[[(3, 5‐dimethylanilino) carbonyl] methyl] phenoxy]‐2‐methylpropionic acid) …

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 …

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 …