Bai Y, Englander S W
Department of Molecular Biology, Scripps Research Institute, LaJolla, California 92037-9701, USA.
Proteins. 1996 Feb;24(2):145-51. doi: 10.1002/(SICI)1097-0134(199602)24:2<145::AID-PROT1>3.0.CO;2-I.
All possible protein folding intermediates exist in equilibrium with the native protein at native as well as non-native conditions, with occupation determined by their free energy level. The study of these forms can illuminate the fundamental principles of protein structure and folding. Hydrogen exchange methods can be used to detect and characterize these partially unfolded forms at native conditions and as a function of mild denaturant and temperature. This information illuminates the requirements that govern the ability of kinetic and equilibrium methods to study folding intermediates.
在天然条件和非天然条件下，所有可能的蛋白质折叠中间体都与天然蛋白质处于平衡状态，其占有率由自由能水平决定。对这些形式的研究可以阐明蛋白质结构和折叠的基本原理。氢交换方法可用于在天然条件下以及作为温和变性剂和温度的函数来检测和表征这些部分展开的形式。这些信息阐明了动力学和平衡方法研究折叠中间体能力的相关要求。
