Cold denaturation of encapsulated ubiquitin.
Cold denaturation of encapsulated ubiquitin.
复制标题
封装泛素的冷变性。
DOI：
10.1021/ja0628654
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发表时间：
2006
影响因子：
15
通讯作者：
Wand,AJoshua
中科院分区：
文献类型：
--
作者：
Pometun,MaximS;Peterson,RonaldW;Babu,CharlesR;Wand,AJoshua
理论上的考虑表明，蛋白质冷变性可以潜在地提供一种手段，探索蛋白质的合作亚结构。蛋白质的冷变性通常预计在水的冰点以下发生。在这里，我们使用包封在溶解在低粘度烷烃中的反胶束中的泛素的NMR光谱来跟踪温度低于−25 °C时冷诱导的解折叠。在各种反胶束缓冲体系中冷诱导的结构转变的比较表明，蛋白质-表面活性剂的相互作用是可以忽略不计的，并允许直接观察的多态冷诱导的蛋白质展开。
Theoretical considerations suggest that protein cold denaturation can potentially provide a means to explore the cooperative substructure of proteins. Protein cold denaturation is generally predicted to occur well below the freezing point of water. Here NMR spectroscopy of ubiquitin encapsulated in reverse micelles dissolved in low viscosity alkanes is used to follow cold-induced unfolding to temperatures below −25 °C. Comparison of cold-induced structural transitions in a variety of reverse micelle-buffer systems indicate that protein−surfactant interactions are negligible and allow the direct observation of the multistate cold-induced unfolding of the protein.