Transmembrane allosteric coupling is a feature of many critical biological signaling events. Here we test whether transmembrane allosteric coupling controls the potassium binding affinity of the prototypical potassium channel KcsA in the context of C-type inactivation. Activation of KcsA is initiated by proton binding to the pH gate upon an...

中文翻译：

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使用固态NMR探测离子通道KcsA的组成性开放突变体中的变构偶联[生物物理学和计算生物学]

跨膜变构偶联是许多关键生物学信号事件的特征。在这里，我们测试了跨膜变构偶联是否在C型失活的情况下控制了原型钾通道KcsA的钾结合亲和力。KcsA的激活通过质子结合到pH门上而启动。