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在0.01 mol.L-1Hepes,0.15 mol.L-1NaCl,pH 7.4及室温条件下,通过荧光光谱、圆二色光谱和紫外差光谱的方法研究了Sm3+与八肋游仆虫中心蛋白C端半分子(C-terminal domain of Euplotes octocarinatus centrin,C-EoCen)III,IV结合位点的结合能力及结合后对蛋白质构象的影响。结果表明,Sm3+与C-EoCen结合后,蛋白质从关闭式构象转变为开放式构象,蛋白的疏水性结构域外露程度增强,同时蛋白的α-螺旋含量明显增大;Sm3+与C-EoCen的III,IV结合位点的条件稳定常数分别为:lgKIII=6.23±0.39,lgKIV=6.81±0.51。
The effects of Sm3 + on the C terminus of C. elegans center protein were studied by fluorescence spectroscopy, circular dichroism spectroscopy and ultraviolet difference spectroscopy in 0.01 mol.L-1Hepes, 0.15 mol.L-1NaCl, pH 7.4 and room temperature conditions. (C-terminal domain of Euplotes octocarinatus centrin, C-EoCen) binding capacity of III and IV binding sites and the effect on protein conformation after binding. The results showed that after the binding of Sm3 + and C-EoCen, the protein changed from a closed conformation to an open conformation, and the hydrophobic domain of the protein was exposed to a greater extent and the α-helix content of the protein was significantly increased. Sm3 + , The stability constants of IV binding sites were: lgKIII = 6.23 ± 0.39, lgKIV = 6.81 ± 0.51.