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Medientyp: E-Artikel Titel: Crowding and the polymerization of sickle hemoglobin Beteiligte: Ferrone, Frank A.; Rotter, Maria A. Erschienen: Wiley, 2004 Erschienen in: Journal of Molecular Recognition, 17 (2004) 5, Seite 497-504 Sprache: Englisch DOI: 10.1002/jmr.698 ISSN: 0952-3499; 1099-1352 Schlagwörter: Molecular Biology ; Structural Biology Entstehung: Anmerkungen: Beschreibung: <jats:title>Abstract</jats:title><jats:p>Under physiological conditions, sickle hemoglobin, a natural mutant of human hemoglobin A with a surface hydrophobic valine in place of a negatively charged glutamic acid, polymerizes at high volume occupancy. Equilibrium solubility of sickle hemoglobin entails activity coefficients that can approach 10<jats:sup>3</jats:sup> at high concentrations. Polymerization occurs by homogeneous and heterogeneous nucleation mechanisms, which are both profoundly sensitive to crowding; homogeneous nucleation rates for example are enhanced by 10<jats:sup>10</jats:sup> when the initial concentration is augmented by 50% non‐polymerizing hemoglobin. A molecular description of the reaction therefore entails substantial corrections for molecular crowding which are all very accurately described by excluded volume corrections, treating hemoglobin as a hard sphere with volume consistent with the molecular structure of the molecule, and involving no further adjustable parameters. These effects and the descriptions that rationalize this behavior are described. Copyright © 2004 John Wiley & Sons, Ltd.</jats:p>