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Universality of supersaturation in protein-fiber formation
Journal article   Open access   Peer reviewed

Universality of supersaturation in protein-fiber formation

Troy Cellmer, Frank A Ferrone and William A Eaton
Nature structural & molecular biology, v 23(5), pp 459-461
May 2016
DOI: https://doi.org/10.1038/nsmb.3197
PMID: 27018803
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://europepmc.org/articles/pmc7329141View
Accepted (AM)Open Access (License Unspecified),  Open

Abstract

Hemoglobin, Sickle - chemistry Humans Kinetics Models, Molecular Protein Aggregates Solubility Thermodynamics
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.

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26 citations in Web of Science
26 citations in Scopus

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
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