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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >Low entropic barrier to the hydrophobic collapse of the prion protein: Effects of intermediate states and conformational flexibility
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Low entropic barrier to the hydrophobic collapse of the prion protein: Effects of intermediate states and conformational flexibility

机译：en病毒疏水性破坏的低熵屏障：中间状态和构象柔韧性的影响

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摘要

A simple kinetic model is applied to study the folding reaction of the C-terminal domain of the murine prion protein, mPrP(121-231). The model provides an equation linking a protein's folding rate with its native topology and the conformational entropic cost of folding. The model predicts that the average conformational entropic cost per residue associated with the folding transition of mPrP(121-231) is smaller than the average for a broad sample of two-state folding proteins. The results are consistent with the native state of mPrP(121-231) being more flexible than the average protein, but the behavior could also arise from the presence of early intermediate states. The findings are in agreement with experimental and theoretical results on the prion protein conformational flexibility. The model is fully analytical and provides a simple way to obtain a quantitative measure of conformational flexibility in two-state proteins from kinetic and structural experimental data.
机译：一个简单的动力学模型用于研究鼠the病毒蛋白mPrP（121-231）C端结构域的折叠反应。该模型提供了一个方程，将蛋白质的折叠速率与其天然拓扑和折叠的构象熵成本联系起来。该模型预测，与mPrP（121-231）的折叠转变相关的每个残基的平均构象熵成本小于两种状态折叠蛋白样本的平均值。结果与mPrP（121-231）的天然状态比平均蛋白更灵活相符，但这种行为也可能是由于早期的中间状态而引起的。这些发现与the病毒蛋白构象柔韧性的实验和理论结果相符。该模型是完全分析的，并且提供了一种简单的方法，可以从动力学和结构实验数据中获得定量测量两种状态蛋白质构象柔性的方法。

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