螺旋-卷曲转变模型中的溶剂效应可以解释内在无序蛋白的异常生物物理
Solvent Effects in the Helix-Coil Transition Model can explain the Unusual Biophysics of Intrinsically Disordered Proteins
摘要：
我们分析了一个模型的统计描述的多肽链螺旋线圈过渡，在那里我们考虑到其主要序列的特异性，量化的相空间体积比的数量对应于螺旋构象的所有可访问的状态。然后将所得的过渡相图与内在无序蛋白（IDP）中二级结构的不寻常行为并列，并观察到许多相似之处，即使蛋白质折叠是一个比螺旋-卷曲过渡更复杂的过渡。事实上，在IDP中观察到的大体积和疏水性氨基酸的缺陷，转化为相空间体积的较大值，使我们能够定位螺旋-卷曲转变的参数空间中的区域，该区域对应于IDP中构象转变固有的二级结构转变，并且与球状蛋白相比，其特征在于修改的相图。在这里，我们认为如何修改的相图的性质，从一个模型的螺旋线圈过渡在溶剂中，将照亮了转出响应的IDP的环境条件的变化，直接遵循从折返（冷变性）分支在他们的折叠相图。
英文摘要：
We analyze a model statistical description of the polypeptide chain helix-coil transition, where we take into account the specificity of its primary sequence, as quantified by the phase space volume ratio of the number of all accessible states to the number corresponding to a helical conformation. The resulting transition phase diagram is then juxtaposed with the unusual behavior of the secondary structures in Intrinsically Disordered Proteins (IDPs) and a number of similarities are observed, even if the protein folding is a more complex transition than the helix-coil transition. In fact, the deficit in bulky and hydrophobic amino acids observed in IDPs, translated into larger values of phase space volume, allows us to locate the region in parameter space of the helix-coil transition that would correspond to the secondary structure transformations that are intrinsic to conformational transitions in IDPs and that is characterized by a modified phase diagram when compared to globular proteins. Here, we argue how the nature of this modified phase diagram, obtained from a model of the helix-coil transition in a solvent, would illuminate the turned-out response of IDPs to the changes in the environment conditions that follow straightforwardly from the re-entrant (cold denaturation) branch in their folding phase diagram.
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