The thermodynamics and kinetics of the aggregation of sickle-cell hemoglobin into fibers
have been studied in great detail under a wide range of solution conditions. The stability of …

Specific ligation states of hemoglobin are, when crystallized, capable of taking on multiple
quaternary structures. The relationship between these structures, captured in crystal lattices …

The role of Lys-95 (β), which is on the exterior of the hemoglobin (HbS) tetramer, in the
aggregation process has been addressed because there is a lack of agreement on its …

The polymerization properties of the fully liganded fluoromet derivative of hemoglobin S
(FmetHb S) were investigated by electron microscopy and absorption spectroscopy …

The kinetics of deoxyhemoglobin S gelation have been investigated using photolytic
dissociation of the carbon monoxide complex to initiate the process. Measurements over a …

The kinetics of ligand rebinding have been studied for modified or cross‐linked hemoglobins
(Hbs). Several compounds were tested that interact with α Val 1 or involve a cross‐link …

Publisher Summary Although the adult human hemoglobin is the most thoroughly studied
protein and arguably one of the best understood, in terms of its function, the methods and …

William N. Poillon* abstract: The effects of three classes of organic cosolvents (aliphatic
alcohols, amides, and ureas) on the gelation of deoxygenated sickle hemoglobin (deoxy-Hb …

For partially ligated cyanomet hemoglobins, Smith and Ackers (Proc. Natl. Acad. Sci. USA 71
(1985) 4312) determined the free energies of dimer-tetramer assembly for all of the partially …