APPLICATION OF PHYSICAL ORGANIC-CHEMISTRY TO ENGINEERED MUTANTS OF PROTEINS - HAMMOND POSTULATE BEHAVIOR IN THE TRANSITION-STATE OF PROTEIN-FOLDING
APPLICATION OF PHYSICAL ORGANIC-CHEMISTRY TO ENGINEERED MUTANTS OF PROTEINS - HAMMOND POSTULATE BEHAVIOR IN THE TRANSITION-STATE OF PROTEIN-FOLDING
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DOI：
10.1073/pnas.90.16.7814
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发表时间：
1993-08-15
影响因子：
11.1
通讯作者：
FERSHT, AR
中科院分区：
文献类型：
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作者：
MATOUSCHEK, A;FERSHT, AR
蛋白质折叠的过渡态可以用线性自由能关系（LFERs）来分析，类似于反应性随结构变化的Bronsted方程。在蛋白质折叠中还有一个额外的lfe来源：变性剂对平衡和速率常数的扰动。这些lfe给出了过渡态在反应坐标上的位置。通过蛋白质工程改变结构和变性剂扰动两种lfer方法分析了藤本酶折叠/展开的过渡态。这种结合使得直接监测反应途径上过渡态的哈蒙德假设行为成为可能。已经发现并分析了过渡态的运动，以提供蛋白质折叠事件顺序的进一步细节。
Transition states in protein folding may be analyzed by linear free-energy relationships (LFERs) analogous to the Bronsted 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.