Solution NMR is a key tool to study intrinsically disordered proteins (IDPs), whose importance for biological function is widely accepted. However, disordered proteins are not limited to solution and are also found in non-soluble systems such as fibrils and membrane proteins. In this Trends article, I will discuss how solid-state NMR can be used to study disorder in non-soluble proteins. Techniques based on dipolar couplings can study static protein disorder which either occurs naturally as e.g. in spider silk or can be induced by freeze trapping IDPs or unfolded proteins. In this case, structural ensembles are directly reflected by a static distribution of dihedral angels that can be determined by the distribution of chemical shifts or other methods. Techniques based on J-couplings can detect dynamic protein disorder under MAS. In this case, only average chemical shifts are measured but disorder can be characterized with a variety of data including secondary chemical shifts, relaxation rates, paramagnetic relaxation enhancements, or residual dipolar couplings. I describe both technical aspects and examples of solid-state NMR on protein disorder and end the article with a discussion of challenges and opportunities of this emerging field.

溶液核磁共振是研究本质无序蛋白质 (IDP) 的关键工具，其对生物功能的重要性已被广泛接受。然而，无序蛋白质不仅限于溶液，也存在于非可溶性系统中，例如原纤维和膜蛋白。在这篇趋势文章中，我将讨论如何使用固态核磁共振来研究不溶性蛋白质的紊乱。基于偶极耦合的技术可以研究静态蛋白质紊乱，这种蛋白质紊乱可以自然发生，例如在蜘蛛丝中，也可以通过冷冻捕获IDP或未折叠蛋白质来诱导。在这种情况下，结构系综直接由二面角的静态分布反映，该静态分布可以通过化学位移的分布或其他方法来确定。基于 J 耦合的技术可以检测 MAS 下的动态蛋白质紊乱。在这种情况下，仅测量平均化学位移，但可以通过各种数据来表征无序，包括二次化学位移、弛豫速率、顺磁弛豫增强或残余偶极耦合。我描述了蛋白质无序固态核磁共振的技术方面和示例，并在文章结尾讨论了这一新兴领域的挑战和机遇。