Radiolytic Footprinting Reveals Conformational Changes During Potassium Channel Gating

Radiolytic Footprinting Reveals Conformational Changes During Potassium Channel Gating

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Gupta, S, D'Mello, R, Chance, MR, Bavro, V, Venien-Bryan, C, Tucker, S
التنسيق:	Journal article
منشور في:	2010

مواد مشابهة

Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry.
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Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating
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Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating.
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Crystal Structure of a Prokaryotic Kir Channel in an Open Conformation
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Role of aromatic localization in the gating process of a potassium channel.
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Role of aromatic localization in the gating process of a potassium channel.
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Conformational changes and gating at the selectivity filter of potassium channels.
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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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H bonding at the helix-bundle crossing controls gating in Kir potassium channels.
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