Role of aromatic localization in the gating process of a potassium channel.
Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for tr...
المؤلفون الرئيسيون: | Domene, C, Vemparala, S, Klein, M, Vénien-Bryan, C, Doyle, D |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2006
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مواد مشابهة
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Role of aromatic localization in the gating process of a potassium channel.
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Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
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Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
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Conformational changes and gating at the selectivity filter of potassium channels.
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