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首页> 美国卫生研究院文献>Biophysical Journal >Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations
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Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations

机译：SARS-CoV核​​壳蛋白N末端RNA结合域的热稳定性：实验和数值模拟

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Differential scanning calorimetry, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and numerical simulations were used to study the thermostability of the N-terminal RNA-binding domain (RBD) of the SARS-CoV nucleocapsid protein. The transition temperature of the RBD in a mixing buffer, composed of glycine, sodium acetate, and sodium phosphate with 100 mM sodium chloride, at pH 6.8, determined by differential scanning calorimetry and circular dichroism, is 48.74°C. Experimental results showed that the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90%. Using a simple Gō-like model and Langevin dynamics we have shown that, in agreement with our experiments, the folding of the RBD is two-state. Theoretical estimates of thermodynamic quantities are in reasonable agreement with the experiments. Folding and thermal unfolding pathways of the RBD also were experimentally and numerically studied in detail. It was shown that the strand β1 from the N-terminal folds last and unfolds first, while the remaining β-strands fold/unfold cooperatively.
机译：差示扫描量热法，圆二色光谱，核磁共振光谱和数值模拟用于研究SARS-CoV核​​衣壳蛋白N端RNA结合域（RBD）的热稳定性。通过差示扫描量热法和圆二色性测定，在由甘氨酸，乙酸钠和磷酸钠与100 mM氯化钠组成的混合缓冲液中，RBD的转变温度为6.8，为pH 6.8。实验结果表明，RBD的热诱导展开-折叠转变遵循可逆性> 90％的两态模型。使用简单的类似Gō的模型和Langevin动力学，我们已经证明，与我们的实验一致，RBD的折叠是两个状态。热力学量的理论估计与实验合理吻合。还对RBD的折叠和热展开路径进行了实验和数值研究。结果表明，来自N末端的链β1最后折叠，然后首先展开，而其余的β链协同折叠/展开。

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