Journal article
Crowding and the polymerization of sickle hemoglobin
Journal of molecular recognition, v 17(5), pp 497-504
Sep 2004
PMID: 15362110
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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(3) 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(10) 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.
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Details
- Title
- Crowding and the polymerization of sickle hemoglobin
- Creators
- Frank A Ferrone - Department of Physics, Drexel University, Philadelphia, PA 19104, USA. fferrone@drexel.eduMaria A Rotter
- Publication Details
- Journal of molecular recognition, v 17(5), pp 497-504
- Publisher
- Wiley; England
- Grant note
- HL57549 / NHLBI NIH HHS HL58512 / NHLBI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000224157400020
- Scopus ID
- 2-s2.0-4544329005
- Other Identifier
- 991014878103504721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics