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Universal Metastability of Sickle Hemoglobin Polymerization

✍ Scribed by Weijun Weng; Alexey Aprelev; Robin W. Briehl; Frank A. Ferrone


Book ID
116663732
Publisher
Elsevier Science
Year
2008
Tongue
English
Weight
517 KB
Volume
377
Category
Article
ISSN
0022-2836

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Crowding and the polymerization of sickl
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## 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 tha