Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.
In this study, the charge selectivity of staphylococcal alpha-hemolysin (alphaHL), a bacterial pore-forming toxin, is manipulated by using cyclodextrins as noncovalent molecular adapters. Anion-selective versions of alphaHL, including the wild-type pore and various mutants, become more anion selecti...
المؤلفون الرئيسيون: | Gu, L, Dalla Serra, M, Vincent, J, Vigh, G, Cheley, S, Braha, O, Bayley, H |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2000
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مواد مشابهة
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Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
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Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
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