Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids. Such biological samples feature functionally relevant molecular dynamics, which often affect different parts of the sample in different ways. Solid-state NMR experiments' sensitivity to dynamics represents a double-edged sword. On the one hand, it offers a chance to measure dynamics in great detail. On the other hand, certain types of motion lead to signal loss and experimental inefficiencies that at first glance interfere with the application of ssNMR to overly dynamic proteins. Dynamics-based spectral editing (DYSE) ssNMR methods leverage motion-dependent signal losses to simplify spectra and enable the study of sub-structures with particular motional properties.

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隐藏的运动和运动引起的不可见性：固态核磁共振中基于动力学的光谱编辑

固态核磁共振 (ssNMR) 光谱能够对包括淀粉样原纤维、非淀粉样蛋白聚集体、膜相关蛋白和病毒衣壳在内的各种生物组件进行结构表征。此类生物样品具有功能相关的分子动力学特征，通常以不同方式影响样品的不同部分。固态核磁共振实验对动力学的敏感性是一把双刃剑。一方面，它提供了一个非常详细地测量动态的机会。另一方面，某些类型的运动会导致信号丢失和实验效率低下，乍一看会干扰 ssNMR 对过度动态蛋白质的应用。