Structure of the pressure-assisted cold denatured state of ubiquitin.
Structure of the pressure-assisted cold denatured state of ubiquitin.
复制标题
压力辅助冷变性状态泛素的结构。
DOI：
10.1006/bbrc.1997.7308
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Jonas,J
中科院分区：
文献类型：
--
作者：
Nash,DP;Jonas,J
利用高分辨核磁共振技术研究了泛素在水溶液中的压力辅助冷变性状态。测定冷变性蛋白质中骨架酰胺质子的氢交换动力学，以确定其结构。与冷变性核糖核酸酶A和溶菌酶相反，冷变性泛素显示出很少的持久二级结构。泛素的行为支持压力辅助冷变性状态的残余结构和早期折叠中间体的结构之间的关系，如果它们存在的想法。
The pressure-assisted cold denatured state of ubiquitin in aqueous solution was investigated by high resolution NMR. Hydrogen exchange kinetics were measured for backbone amide protons in the cold denatured protein to determine its structure. In contrast to cold denatured ribonuclease A and lysozyme, cold denatured ubiquitin shows little persistent secondary structure. The behavior of ubiquitin supports the idea of a relationship between the residual structure of pressure-assisted cold-denatured states and the structure of early folding intermediates provided they exist.