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Structural Disorder in Viral Proteins

机译：病毒蛋白的结构紊乱

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One of the core standards of biochemistry is that the function of a protein relies on its 3D structure. This idea posits that all the information required for a protein to perform its biological function(s) is contained in its amino acid sequence and that the protein can only carry out these functions once it has been folded into a particular structure.~1 This notion, however, has been challenged over the past 20?25 years due to the finding of a myriad of counterexamples that suggest that many proteins and protein regions in fact possess a partly or entirely disordered structure. These intrinsically disordered proteins (IDPs) or regions (IDRs) do not have a stable or unique 3D structure in solution, in physiological conditions of both pH and salinity, and when lacking a partner. Instead, these proteins exist as dynamic ensembles of conformations that do not have a stable folded structure and still carry out their respective biological activities.~(2?13) Proteins and protein regions involved in the establishment of numerous interactions, such as proteins/regions implicated in signaling, recognition, and regulation activities, are enriched in intrinsic disorder (ID).~(2,5,6,14?23) These and other crucial functional roles explain the high abundance of IDPs in all species.
机译：生物化学的核心标准之一是蛋白质的功能取决于其3D结构。这个想法认为，蛋白质执行其生物学功能所需的所有信息都包含在其氨基酸序列中，并且蛋白质只有将其折叠成特定的结构后才能执行这些功能。〜1这个概念然而，由于发现了众多的反例，这些反例表明许多蛋白质和蛋白质区域实际上具有部分或完全无序的结构，因此在过去的20-25年间一直受到挑战。这些固有的无序蛋白（IDP）或区域（IDR）在溶液中，在pH和盐度的生理条件下以及缺乏伴侣时，都没有稳定或独特的3D结构。取而代之的是，这些蛋白质以动态构象形式存在，这些构象不具有稳定的折叠结构，并且仍然发挥各自的生物学活性。（2？13）参与建立大量相互作用的蛋白质和蛋白质区域，例如蛋白质/区域涉及信号，识别和调节活动的内源性疾病（ID）丰富。〜（2,5,6,14？23）这些及其他重要的功能性作用解释了所有物种中IDP的丰富性。

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