Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation
Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation
复制标题
DOI：
10.1038/nsmb739
复制
发表时间：
2004-04-01
影响因子：
16.8
通讯作者：
Wand, AJ
中科院分区：
文献类型：
--
作者：
Babu, CR;Hilser, VJ;Wand, AJ
蛋白质热力学的现代观点预测蛋白质经历冷诱导的去折叠。不幸的是，蛋白质和水的性质阻碍了对这一基本过程的详细观察。在这里，我们使用蛋白质包封，使冷变性的蛋白质泛素进行监测的高分辨率NMR在温度接近35 degreesC。冷诱导展开的泛素被发现是高度不合作的，在不同的对比，这个和其他蛋白质的热熔化。这些结果表明冷变性作为剖析蛋白质合作亚结构的手段的潜力，并为测试蛋白质稳定性、动力学和功能的统计热力学处理提供严格的框架。
The modern view of protein thermodynamics predicts that proteins undergo cold-induced unfolding. Unfortunately, the properties of proteins and water conspire to prevent the detailed observation of this fundamental process. Here we use protein encapsulation to allow cold denaturation of the protein ubiquitin to be monitored by high-resolution NMR at temperatures approaching 35 degreesC. The cold-induced unfolding of ubiquitin is found to be highly noncooperative, in distinct contrast to the thermal melting of this and other proteins. These results demonstrate the potential of cold denaturation as a means to dissect the cooperative substructures of proteins and to provide a rigorous framework for testing statistical thermodynamic treatments of protein stability, dynamics and function.