Englander S W, Englander J J, McKinnie R E, Ackers G K, Turner G J, Westrick J A, Gill S J
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.
Science. 1992 Jun 19;256(5064):1684-7. doi: 10.1126/science.256.5064.1684.
The inability to localize and measure the free energy of protein structure and structure change severely limits protein structure-function investigations. The local unfolding model for protein hydrogen exchange quantitatively related the free energy of local structural stability with the hydrogen exchange rate of concerted sets of structurally related protons. In tests with a number of modified hemoglobin forms, the loss in structural free energy obtained locally from hydrogen exchange results matches the loss in allosteric free energy measured globally by oxygen-binding and subunit dissociation experiments.
无法定位和测量蛋白质结构及其变化的自由能，这严重限制了蛋白质结构与功能的研究。蛋白质氢交换的局部去折叠模型将局部结构稳定性的自由能与结构相关质子协同组的氢交换速率定量关联起来。在对多种修饰血红蛋白形式的测试中，通过氢交换结果局部获得的结构自由能损失与通过氧结合和亚基解离实验全局测量的变构自由能损失相匹配。
