人源电压门控质子通道C端结构域pH依赖结构特性及热稳定性研究
首发时间:2014-11-15
摘要:目的:人源电压门控质子通道Hv1为同源二聚体,通道蛋白的二聚化及通道活化的温度敏感性与其C端结构域直接相关。为了阐明质子通道的温度敏感机制,本文研究了pH值对Hv1 的C端结构域依赖的结构特性及热稳定性的影响。方法:制备Hv1的C端结构域蛋白,检测该蛋白在不同温度和pH值影响下的圆二色谱。结果:C端结构域二级结构和三级结构的热稳定性在pH 5-8内随着pH值的升高而降低。其热力学参数对pH值敏感,pH 5,6,7和8条件下,该单白Tm值分别是56.4,46.4,44.5和44.6℃。结论:Hv1通道活化的温度敏感性可能与其C端结构域的pH依赖热稳定性直接相关。
关键词: 分子生物学;电压门控质子通道 Hv1;C端结构域;pH依赖;热稳定性
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pH-dependently coiled-coil structural stability of the carboxyl-terminal domain of voltage-gated proton channel Hv1
Abstract:Objective:The C terminus of the voltage-gated proton channel Hv1 is a homodimer with a parallel coiled-coil structure, which is responsible for whole Hv1 protein dimeric architecture and temperature-sensitive activity. To elucidate the mechanism of the temperature-sensitive activity of the proton channel, the pH-dependent structural stability of the C-terminal domain of Hv1 was studied.methods:monitoring the temperature-induced denaturation in rang of pH 5-8 by CD,Size exclusion chromatography and Tryptophyl fluorescence measurements . Results: the secondary structure and thermostability of the protein are decreased with an increasing in pH at a range of pH 5-8. The melting temperature is 56.4, 46.4, 44.5 and 44.6oC for pH 5, 6, 7 and 8, respectively. Furthermore, the other thermodynamic parameters were also sensitive to pH.Conclusion:The thermodynamic properties of the C-terminal domain may contribute to the temperature-dependent activation of Hv1.(10 Points, Times New Roman)
Keywords: Molecular Biophysics Voltage-gated proton channel Hv1 C-terminal domain Coiled-coil pH-dependence Stability
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人源电压门控质子通道C端结构域pH依赖结构特性及热稳定性研究
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