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

The liganded hemoglobin (Hb) high-salt crystallization condition described by Max Perutz
has generated three different crystals of human adult carbonmonoxy hemoglobin (COHbA) …

Dimeric lactoglobulin molecules exist in the open conformation at basic pH, whereas they
exist in the closed conformation at acidic pH, after undergoing the Tanford transition around …

A detailed description of hemoglobin cooperativity requires knowledge of the dimer− dimer
interactions responsible for the low ligand affinity of the quaternary-T tetramer, the …

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 …

Hemoglobin was one of the first protein structures to be determined by X-ray crystallography
and served as a basis for the two-state MWC model for the mechanism of allosteric proteins …

High-salt crystals of human oxy-and deoxyhaemoglobin have been studied at different
levels of environmental humidity and solvent content. The structure of the oxy form remains …

Recent crystallographic studies suggested that fully liganded human hemoglobin can adopt
multiple quaternary conformations that include the two previously solved relaxed …

Although X-ray crystallography is the most commonly used technique for studying the
molecular structure of proteins, it is not generally able to monitor the dynamic changes or …

The crystal structure of high-salt horse methaemoglobin has been determined at
environmental relative humidities (rh) of 88, 79, 75 and 66%. The molecule is in the R state …