Báo cáo khoa học: Vibrio cholerae hemolysin Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity
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Vibrio choleraehemolysin (HlyA), a water-soluble proteinwith a native monomeric relative molecular mass of 65 000,forms transmembrane pentameric channels in target bio-membranes.TheHlyAbinds to lipid vesicles nonspecificallyand without saturation; however, self-assembly is triggeredspecifically by cholesterol.Here we show that the HlyApartitioned quantitatively to amphiphilic media irrespectiveof their compositions, indicating that the toxin had anamphiphilic surface.
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Báo cáo khoa học: Vibrio cholerae hemolysin Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity
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Báo cáo khoa học: Vibrio cholerae hemolysin Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity
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