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从动力学研究中洞察耦合折叠与结合机制。

Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.

作者信息

Shammas Sarah L, Crabtree Michael D, Dahal Liza, Wicky Basile I M, Clarke Jane

机构信息

From the Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom

From the Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.

出版信息

J Biol Chem. 2016 Mar 25;291(13):6689-95. doi: 10.1074/jbc.R115.692715. Epub 2016 Feb 5.

Abstract

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.

摘要

内在无序蛋白(IDP)的特点是缺乏持久的结构。自从十多年前它们被发现以来,许多关于其功能相关性和相互作用机制的问题仍未得到解答。尽管大多数实验都从平衡和结构的角度进行,但较少有研究探讨它们相互作用的动力学。在这里,我们回顾并强调了可以从动力学研究中获得的信息类型。特别是,我们展示了耦合折叠和结合反应(一类重要的信号事件)的动力学研究对于确定机制是如何必要的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4128/4807256/b85fbbbb464f/zbc0121640610001.jpg

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