The amyloid fold is structurally characterized by a typical cross-β architecture, which is under debate to represent an energy-favourable folding state that many globular or natively unfolded proteins can adopt. Being initially solely associated with amyloid fibrils observed in the propagation of several neurodegenerative disorders, the discovery of non-pathological (or “functional”) amyloids in many native biological processes has recently further intensified the general interest invested in those cross-β supramolecular assemblies. The insoluble and non-crystalline nature of amyloid fibrils and their usually inhomogeneous appearance on the mesoscopic level pose a challenge to biophysical techniques aiming at an atomic-level structural characterization. Solid-state NMR spectroscopy (SSNMR) has granted breakthroughs in structural investigations on amyloid fibrils ranging from the assessment of the impact of polymorphism in disease development to the 3D atomic structure determination of amyloid fibrils. First landmark studies towards the characterization of atomic structures and interactions involving functional amyloids have provided new impulses in the understanding of the role of the amyloid fold in native biological functions.

Over the last decade many strategies have been developed in protein isotope labelling, NMR resonance assignment, distance restraint determination and 3D structure calculation of amyloid fibrils based on SSNMR approaches. We will here discuss the emerging concepts and state-of-the-art methods related to the assessment of amyloid structures and interactions involving amyloid entities by SSNMR.

淀粉样蛋白折叠的结构特征是典型的交叉β构架，该构架正在争论以代表许多球形或天然未折叠蛋白可以采用的能量有利的折叠状态。最初仅与在几种神经退行性疾病的传播中观察到的淀粉样蛋白原纤维相关，最近在许多天然生物学过程中发现非病理性（或“功能性”）淀粉样蛋白进一步增强了人们对那些跨β超分子组装体的普遍兴趣。淀粉样原纤维的不溶性和非结晶性及其在介观水平上通常不均一的外观对旨在原子级结构表征的生物物理技术提出了挑战。固态NMR光谱（SSNMR）在淀粉样蛋白原纤维的结构研究中取得了突破，从评估疾病发展中多态性的影响到淀粉样蛋白原纤维的3D原子结构确定。对具有功能性淀粉样蛋白的原子结构和相互作用进行表征的第一个具有里程碑意义的研究为了解淀粉样蛋白折叠在天然生物学功能中的作用提供了新的动力。

在过去的十年中，基于SSNMR方法，在蛋白质同位素标记，NMR共振分配，距离约束测定和淀粉样原纤维的3D结构计算方面已经开发了许多策略。我们将在这里讨论与通过SSNMR评估淀粉样蛋白结构和涉及淀粉样蛋白实体的相互作用有关的新兴概念和最新技术。