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Nonlinearity of a Voltage-Gated Potassium Channel Revealed by the Mechanical Susceptibility

机译:机械敏感性显示电压门控钾通道的非线性

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The voltage-gated potassium channel from Aeropyrum pernix operates by coupling the voltage-driven motion of a charged group of amino acids to the opening and closing of the pore. In this experiment, we drive this charged group with an ac field and observe the effect on the gating. The measurements for different frequencies and amplitudes of the forcing reveal an essential nonlinearity in the mechanical behavior of the molecule. Within a continuum-mechanics description, we extract the effective dissipation parameter γ for this conformational motion and find γ≈0.2??g/s, similar to recent nanorheology measurements on the conformational motion of an enzyme.
机译:Aeropyrum pernix的电压门控钾通道通过将带电荷的氨基酸基团的电压驱动运动耦合到孔的开放和闭合而运行。在本实验中,我们用一个交流场驱动该带电的组,并观察对门控的影响。对强迫的不同频率和幅度的测量揭示了分子的机械行为中的基本非线性。在连续力学的描述中,我们提取了这种构象运动的有效耗散参数γ,并发现γ≈0.2≤g/ s,这类似于最近对酶构象运动的纳米流变学测量。

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