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首页> 外文期刊>Journal of Molecular Biology >Folding energetics of a multidomain protein, flagellin.
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Folding energetics of a multidomain protein, flagellin.

机译：多域蛋白鞭毛蛋白的折叠能量学。

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Thermodynamic investigations of flagellin from Salmonella typhimurium and its proteolytic fragments were conducted by differential scanning calorimetry (DSC) and circular dichroism (CD) melting measurements. A new method of analysis for a multi-state transition based on our original theoretical treatment of thermodynamic equations has been developed to analyze those data. The analysis of DSC curves confirmed the three thermodynamic domains of flagellin. The thermodynamic parameters of each domain were revised from those previously reported and the new values of the parameters have a good correlation to the apparent molecular masses of the morphological domains. CD melting measurements at far and near-UV wavelengths showed sequential unfolding of the domains. Therefore, we could reasonably assign the thermodynamically identified domains to the morphological domains. Further analysis of both DSC and CD data provided insights into the folding energetics of the multidomain structure of flagellin. An inner domain (Df1) of flagellin in the filament unfolds through a relatively broad transition, while the two outer domains unfold cooperatively and show sharp transitions. This indicates that the interdomain interactions between Df1 and D2 has different characteristics from the apparently more intimate interactions between D2 and D3. These characteristics suggest that flagellin is organized with relatively flexible domains and rigid domains, which appears to be responsible for the well-regulated assembly mechanism of the bacterial flagellar filament. Copyright 1999 Academic Press.
机译：鼠伤寒沙门氏菌鞭毛蛋白及其蛋白水解片段的热力学研究通过差示扫描量热法（DSC）和圆二色性（CD）融解法进行。已经开发了一种基于我们对热力学方程的原始理论处理的多态跃迁分析的新方法来分析这些数据。 DSC曲线的分析证实了鞭毛蛋白的三个热力学区域。每个域的热力学参数均已从以前的报告中进行了修订，参数的新值与形态域的表观分子质量具有良好的相关性。在远紫外和近紫外波长下的CD熔解测量显示了域的顺序展开。因此，我们可以合理地将热力学上确定的区域分配给形态区域。 DSC和CD数据的进一步分析为深入了解鞭毛蛋白多域结构的折叠能学提供了见识。细丝中鞭毛蛋白的内部结构域（Df1）通过相对较宽的过渡而展开，而两个外部结构域协同地展开并显示出急剧的过渡。这表明Df1和D2之间的域间交互作用与D2和D3之间似乎更紧密的交互作用具有不同的特征。这些特征表明鞭毛蛋白具有相对柔性的结构域和刚性的结构域，这似乎是细菌鞭毛细丝的良好调节组装机制的原因。版权所有1999，学术出版社。

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