Linking folding and binding.
Linking folding and binding.
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DOI：
10.1016/j.sbi.2008.12.003
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发表时间：
2009-02
影响因子：
6.8
通讯作者：
Dyson, H. Jane
中科院分区：
文献类型：
--
作者：
Wright, Peter E.;Dyson, H. Jane
许多细胞蛋白质本质上是无序的，并且在与其生理靶结合时全部或部分地经历折叠。在过去的几年里，描述内在无序蛋白质（包括自由蛋白质和与靶标结合的蛋白质）特征的论文呈指数级增长。虽然核磁共振光谱仍然是最受欢迎的工具，一些新的生物物理技术被证明是非常有用的，在定义的限制构象合奏。在预测无序蛋白质中的识别元件、阐明耦合折叠和结合过程的动力学和机制以及理解翻译后修饰在调节生物反应中的作用方面取得了进展。在这里，我们回顾这些和其他最近的进展，提供了新的见解的构象倾向和相互作用的内在无序的蛋白质，并开始揭示其生物学功能的一般原则。
Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part, upon binding to their physiological targets. The past few years have seen an exponential increase in papers describing characterization of intrinsically disordered proteins, both free and bound to targets. Although NMR spectroscopy remains the favored tool, a number of new biophysical techniques are proving exceptionally useful in defining the limits of the conformational ensembles. Advances have been made in prediction of the recognition elements in disordered proteins, in elucidating the kinetics and mechanism of the coupled folding and binding process, and in understanding the role of post-translational modifications in tuning the biological response. Here we review these and other recent advances that are providing new insights into the conformational propensities and interactions of intrinsically disordered proteins and are beginning to reveal general principles underlying their biological functions.
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影响因子：
64.8
作者：
Demarest, SJ;Martinez-Yamout, M;Wright, PE
通讯作者：
Wright, PE
影响因子：
15
作者：
Bonsor, Daniel A.;Grishkovskaya, Irina;Kleanthous, Colin
通讯作者：
Kleanthous, Colin
影响因子：
4.8
作者：
Chong, PA;Ozdamar, B;Forman-Kay, JD
通讯作者：
Forman-Kay, JD
影响因子：
5.6
作者：
De Guzman, RN;Goto, NK;Wright, PE
通讯作者：
Wright, PE
影响因子：
16.8
作者：
Baker, Jennifer M. R.;Hudson, Rhea P.;Forman-Kay, Julie D.
通讯作者：
Forman-Kay, Julie D.