Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.
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对动力学研究的耦合折叠和结合机制的见解。
DOI：
10.1074/jbc.r115.692715
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发表时间：
2016-03-25
期刊：
影响因子：
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通讯作者：
Clarke J
中科院分区：
文献类型：
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作者：
Shammas SL;Crabtree MD;Dahal L;Wicky BI;Clarke J
内含子无序蛋白（IDP）的特征在于缺乏持久的结构。自十多年前确定以来，关于其功能相关性和互动机制的许多问题仍然没有答案。虽然大多数实验都采取了平衡和结构的观点，很少有研究调查他们的相互作用的动力学。在这里，我们回顾和强调的类型的信息，可以从动力学研究。特别是，我们展示了如何动力学研究耦合折叠和结合反应，一类重要的信号事件，需要确定机制。
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions regarding their functional relevance and interaction mechanisms remain unanswered. Although most experiments have taken equilibrium and structural perspectives, fewer studies have investigated the kinetics of their interactions. Here we review and highlight the type of information that can be gained from kinetic studies. In particular, we show how kinetic studies of coupled folding and binding reactions, an important class of signaling event, are needed to determine mechanisms.