title: Universality of supersaturation in protein-fiber formation.
abstract: 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 the fiber is measured by the solubility; the kinetics is characterized by a delay before the appearance of fibers. A review of data in the literature shows that there is no correlation of the delay time with fiber stability and only a weak correlation with the initial protein concentration. There is, however, a striking collapse of all the data onto a single universal curve when the delay time is plotted versus the supersaturation, which is the ratio of the initial protein concentration to the solubility, expressed as activities. Collapse onto the same universal curve is also obtained when using delay times calculated from the double-nucleation theoretical model.
authors.affiliation: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
authors.forename: Troy
authors.initials: T
authors.lastname: Cellmer
authors.affiliation: Department of Physics, Drexel University, Philadelphia, Pennsylvania, USA.
authors.forename: Frank A
authors.initials: FA
authors.lastname: Ferrone
authors.affiliation: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
authors.forename: William A
authors.initials: WA
authors.lastname: Eaton
mesh_terms: D006451:Hemoglobin, Sickle / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D066329:Protein Aggregates; D012995:Solubility; D013816:Thermodynamics
chemical_list: D006451:Hemoglobin, Sickle; D066329:Protein Aggregates