物理有机化学在蛋白质工程突变体中的应用：蛋白质折叠过渡态中的哈蒙德假说行为
Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding.
作者信息
Matouschek A, Fersht A R
机构信息
Cambridge Centre for Protein Engineering, University Chemical Laboratory, United Kingdom.
出版信息
Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7814-8. doi: 10.1073/pnas.90.16.7814.
Abstract
Transition states in protein folding may be analyzed by linear free-energy relationships (LFERs) analogous to the Brønsted equation for changes in reactivity with changes in structure. There is an additional source of LFERs in protein folding: the perturbation of the equilibrium and rate constants by denaturants. These LFERs give a measure of the position of the transition state along the reaction coordinate. The transition state for folding/unfolding of barnase has been analyzed by both types of LFERs: changing the structure by protein engineering and perturbation by denaturants. The combination has allowed the direct monitoring of Hammond postulate behavior of the transition state on the reaction pathway. Movement of the transition state has been found and analyzed to give further details of the order of events in protein folding.
摘要
蛋白质折叠过程中的过渡态可以通过线性自由能关系（LFERs）进行分析，这类似于描述反应性随结构变化的布朗斯特方程。在蛋白质折叠中，LFERs还有另一个来源：变性剂对平衡常数和速率常数的扰动。这些LFERs可以衡量过渡态在反应坐标上的位置。通过两种类型的LFERs对核糖核酸酶 barnase的折叠/去折叠过渡态进行了分析：通过蛋白质工程改变结构以及通过变性剂进行扰动。这种结合使得能够直接监测过渡态在反应途径上的哈蒙德假说行为。已经发现并分析了过渡态的移动情况，以进一步了解蛋白质折叠过程中事件发生的顺序细节。
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