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

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)