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Introduction to Intrinsically Disordered Proteins (IDPs)

机译：固有紊乱蛋白（IDP）简介

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For more than a century, molecular and structural biology, biochemistry, and protein biophysics have been dominated by a "rigid" or "semi-rigid" view of a functional protein molecule or functional protein domain. These functional entities were assumed to possess unique and stable 3D structures, a view supported by numerous reports of protein structures determined using X-ray crystallography and NMR spectroscopy (as of May 27, 2014, there were 97,857 structures of proteins and protein-nucleic acid complexes in the Protein Data Bank, with 87,536 of these structures (89.5%) determined by X-ray crystallography). These experimentally determined structures depicted protein molecules as aperiodic crystals, in which both atoms and backbone Ramachandran angles are relatively fixed and possess low-amplitude thermal fluctuations around their equilibrium positions. Although the functions of many proteins clearly fit within this structure?function paradigm, where a unique amino acid sequence encodes a unique energetically stable 3D fold associated with conformational fluctuations that allow for unique biological function, recent studies have revealed that many functional proteins or functional protein regions do not have unique 3D structures under functional conditions. In fact, contrarily to the ordered proteins and domains, such biologically active intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) have no single, well-defined equilibrium structure and exist as highly dynamic, heterogeneous ensembles of conformers resulting from their relatively flat free-energy surface.
机译：一个多世纪以来，分子和结构生物学，生物化学和蛋白质生物物理学一直被功能蛋白分子或功能蛋白域的“刚性”或“半刚性”观点所主导。假定这些功能实体具有独特且稳定的3D结构，这一观点得到了许多使用X射线晶体学和NMR光谱法测定的蛋白质结构的报告的支持（截至2014年5月27日，蛋白质和蛋白质核酸的结构为97,857个）蛋白质数据库中的复合物，其中X射线晶体学测定的这些结构中有87,536个（占89.5％）。这些实验确定的结构将蛋白质分子描绘为非周期性晶体，其中原子和骨架Ramachandran角均相对固定，并且在其平衡位置附近具有低振幅的热涨落。尽管许多蛋白质的功能显然适合这种结构-功能范例，其中独特的氨基酸序列编码与构象波动相关的独特的能量稳定3D折叠，从而允许独特的生物学功能，但最近的研究表明，许多功能蛋白或功能蛋白区域在功能条件下没有独特的3D结构。实际上，与有序蛋白质和结构域相反，此类具有生物活性的内在无序蛋白（IDP）和内在无序蛋白区域（IDPR）没有单一的，定义明确的平衡结构，并以高动态性，异质性的构象体形式存在相对平坦的自由能表面。

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