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首页> 外文期刊>Biophysical Journal >Probing conformational changes of prestin with thiol-reactive optical switches.
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Probing conformational changes of prestin with thiol-reactive optical switches.

机译：用硫醇反应性光学开关探测蛋白的构象变化。

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摘要

Thiol-reactive optical switch probes were used to examine conformational changes of prestin-based membrane motor. Because this motor is based on mechanoelectric coupling similar to piezoelectricity, the motile activity can be monitored by charge movements across the plasma membrane, which appears as nonlinear capacitance. When the plasma membrane is conjugated with the probes, optically induced spiro-merocyanine transition positively shifted nonlinear capacitance of outer hair cells and prestin-transfected cells by approximately 10 mV. These shifts were reversible and were eliminated by pretreatment with iodoacetamide. However, they were little affected by pretreatment with biotin maleimide, which cannot reach the cytoplasmic surface. Our results showed that merocyanine states, with a larger dipole moment, interact with the motor's extended conformation stronger than with the compact conformation by 1.6 x 10(-21) J/molecule. The interaction sites are near the cytoplasmic side of the motor protein.
机译：硫醇反应性光开关探针用于检查基于Prestin的膜运动蛋白的构象变化。由于此电动机基于类似于压电的机械电耦合，因此可以通过质膜上的电荷运动来监测运动活动，该运动表现为非线性电容。当质膜与探针结合时，光学诱导的螺-花青素跃迁将外部毛细胞和经prestin转染的细胞的非线性电容正向移动约10 mV。这些变化是可逆的，并通过碘乙酰胺预处理得以消除。然而，它们很少受到无法到达细胞质表面的生物素马来酰亚胺预处理的影响。我们的结果表明，具有更高偶极矩的部花菁态与电机的扩展构象相互作用比与紧凑构象的相互作用强1.6 x 10（-21）J /分子。相互作用位点在运动蛋白的细胞质侧附近。

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