Ellis L M
Biophys J. 1978 Jul;23(1):79-87. doi: 10.1016/S0006-3495(78)85434-4.
The kinetics of hydrogen exchange from folded proteins can be molded as a function of two continuous distributions of rate constants, kcx and kn, representing exchange from the folded and unfolded conformations, respectively. This model can account for the temperature dependence of soybean trypsin inhibitor at pH 3 and pH 6.5. The physical significance of this model, especially the shape and breadth of the kn distribution, are discussed.
折叠蛋白质中氢交换的动力学可以被构建为速率常数kcx和kn两个连续分布的函数，分别代表折叠态和非折叠态构象的交换。该模型可以解释大豆胰蛋白酶抑制剂在pH 3和pH 6.5时的温度依赖性。本文讨论了该模型的物理意义，特别是kn分布的形状和宽度。
