Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding
Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding
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DOI：
10.1016/s0301-4622(02)00294-6
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发表时间：
2003-01-01
影响因子：
3.8
通讯作者：
Kiefhaber, T
中科院分区：
文献类型：
--
作者：
Sánchez, IE;Kiefhaber, T
在蛋白质折叠反应中经常观察到突变或溶剂条件变化时的非线性速率平衡关系，并且通常用哈蒙德行为来解释。本文首先对化学反应中过渡态运动的概念进行了概述，并讨论了它在蛋白质折叠中的应用。然后，我们展示了真正的哈蒙德的行为和明显的过渡态运动所造成的其他影响，如在限速步骤的折叠反应或基态效应，即结构变化的天然状态或未折叠状态的变化。这些例子表明，明显的过渡态运动很容易被误认为是Hamnion行为。我们描述了实验测试，使用自我和交叉相互作用参数，以区分结构的变化，在一个单一的过渡态以下哈蒙德的行为和明显的过渡态运动所造成的其他影响。(C)2002爱思唯尔科技有限公司。保留所有权利。
Non-linear rate-equilibrium relationships upon mutation or changes in solvent conditions are frequently observed in protein folding reactions and are usually interpreted in terms of Hammond behavior. Here we first give a general overview over the concept of transition state movements in chemical reactions and discuss its application to protein folding. We then show examples for genuine Hammond behavior and for apparent transition state movements caused by other effects like changes in the rate-limiting step of the folding reaction or ground state effects, i.e. structural changes in either the native state or the unfolded state. These examples show that apparent transition state movements can easily be mistaken for Hamniond behavior. We describe experimental tests using self- and cross-interaction parameters to distinguish between structural changes in a single transition state following Hammond behavior and apparent transition state movements caused by other effects. (C) 2002 Elsevier Science B.V. All rights reserved.