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...
Hlavní autoři: | Gu, L, Dalla Serra, M, Vincent, J, Vigh, G, Cheley, S, Braha, O, Bayley, H |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2000
|
Podobné jednotky
-
A functional protein pore with a "retro" transmembrane domain.
Autor: Cheley, S, a další
Vydáno: (1999) -
Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules.
Autor: Movileanu, L, a další
Vydáno: (2001) -
Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore.
Autor: Gu, L, a další
Vydáno: (2003) -
Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
Autor: Gouaux, J, a další
Vydáno: (1994) -
Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
Autor: Miles, G, a další
Vydáno: (2002)