From sequence and forces to structure, function, and evolution of intrinsically disordered proteins.
From sequence and forces to structure, function, and evolution of intrinsically disordered proteins.
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DOI：
10.1016/j.str.2013.08.001
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发表时间：
2013-09-03
期刊：
影响因子：
--
通讯作者：
Mittag T
中科院分区：
文献类型：
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作者：
Forman-Kay JD;Mittag T
缺乏持久结构的固有无序蛋白质(IDPs)是结构生物学的一个挑战，因为折叠蛋白质的标准方法不适用，而且它们偏离了主导的结构/功能范式。然而，它们的广泛存在和对生物功能的参与促使人们越来越多地接受国内流离失所者的重要性，并开发新的工具来研究其结构、动态和功能。折叠和无序的功能结构域或区域的相互作用，以及蛋白质状态相对于构象能量学、运动时标和紧凑性的存在，正在形成对结构-动力学-无序/功能关系的统一理解。在这本期刊《结构》出版20周年之际，我们对国内流离失所者的调查进行了历史回顾，并总结了其独特的结构、功能和进化特性背后的序列特征和物理力量。
Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to structural biology due to the inapplicability of standard methods for characterization of folded proteins as well as their deviation from the dominant structure/function paradigm. Their widespread presence and involvement in biological function, however, has spurred the growing acceptance of the importance of IDPs and the development of new tools for studying their structure, dynamics and function. The interplay of folded and disordered domains or regions for function and the existence of a continuum of protein states with respect to conformational energetics, motional timescales and compactness is shaping a unified understanding of structure-dynamics-disorder/function relationships. On the 20th anniversary of this journal, Structure, we provide a historical perspective on the investigation of IDPs and summarize the sequence features and physical forces that underlie their unique structural, functional and evolutionary properties.