The extraordinary flexibility and structural heterogeneity of intrinsically disordered proteins (IDP) make them functionally versatile molecules. We have now begun to better understand their fundamental role in biology, however many aspects of their behaviour remain difficult to grasp experimentally. This is especially true for the intermolecular interactions which lead to the formation of transient or highly dynamic supramolecular self-assemblies, such as oligomers, aggregation intermediates and biomolecular condensates. Both the emerging functions and pathogenicity of these structures have stimulated great efforts to develop methodologies capable of providing useful insights. Significant progress in solution NMR spectroscopy has made this technique one of the most powerful to describe structural and dynamic features of IDPs within such assemblies at atomic resolution. Here, we review the most recent works that have illuminated key aspects of IDP assemblies and contributed significant advancements towards our understanding of the complex conformational landscape of prototypical disease-associated proteins. We also include a primer on some of the fundamental and innovative NMR methods being used in the discussed studies.

中文翻译：

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溶液NMR深入了解了无序淀粉样蛋白的动态超分子组装。

本质上无序的蛋白质（IDP）的非凡灵活性和结构异质性使其成为功能上通用的分子。现在我们已经开始更好地了解它们在生物学中的基本作用，但是它们的行为的许多方面仍然很难通过实验来掌握。对于导致瞬时或高度动态的超分子自组装体形成的分子间相互作用，尤其如此，例如低聚物，聚集中间体和生物分子缩合物。这些结构的新兴功能和致病性都激发了人们的巨大努力，以开发能够提供有用见解的方法。溶液NMR光谱学的重大进展已使这项技术成为描述原子组装中此类组件中IDP的结构和动态特征的最强大工具之一。在这里，我们回顾了最新的著作，这些著作阐明了IDP组装的关键方面，并为我们对原型疾病相关蛋白的复杂构象格局的理解做出了重大贡献。我们还将介绍所讨论研究中使用的一些基本和创新NMR方法的入门知识。