Hemoglobin (Hb) is an essential component of the circulatory system of vertebrates. Its chief
physiological function is to transport oxygen from the lungs to the tissues. For reviews of the …

Molecular biologists and biochemists have long been intrigued by the concept of molecular
codes for the structure and function of biological macromolecules, ie, a set of rules which …

Although tetrameric hemoglobin has been studied extensively as a prototype for
understanding mechanisms of allosteric regulation, the functional and structural properties …

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

Publisher Summary This chapter emphasizes the molecular basis of the cooperative
oxygenation of human normal adult hemoglobin (Hb A). Various experimental results …

Spectroelectrochemical techniques are described which enable us to compare anion effects
on redox curves of structurally distinct hemoglobins with oxygenation curves obtained under …

The primary role for erythrocytes is oxygen transport that requires the reversible binding of
oxygen to hemoglobin. There are, however, secondary reactions whereby the erythrocyte …

Calcium-dependent conformational states of calmodulin (CaM) were probed by thrombin to
determine quantitative differences in the susceptibility of two bonds: Arg37− Ser38 (R37 …

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 …

Hemoglobins achieve cooperative oxygen binding by diverse strategies based on different
assemblies of globin subunits. Heterotetrameric hemoglobin from Scapharca inaequivalvis …