Abstract：
In vivo, protein aggregation arises due to incorrect folding or misfolding. The aggregation of proteins into amyloid fibrils is the characteristic feature of various misfolding diseases known as amyloidosis, such as Alzheimer\'s and Parkinson\'s disease. The heterogeneous nature of these fibrils restricts the extent to which their structure may be characterized. Advancements in techniques, such as X-ray diffraction, cryo-electron microscopy, and solid-state NMR have yielded intricate insights into structures of different amyloid fibrils. These studies have unveiled a diverse range of polymorphic structures that typically conform to the cross-β amyloid pattern. This chapter provides a concise overview of the information acquired in the field of protein aggregation, with particular focus on amyloids.
摘要：
在体内,蛋白质聚集是由于不正确的折叠或错误折叠而产生的。蛋白质聚集成淀粉样纤维是各种错误折叠疾病的特征，称为淀粉样变性。如老年痴呆症和帕金森氏症。这些原纤维的异质性质限制了其结构可被表征的程度。技术的进步，如X射线衍射，低温电子显微镜，和固态NMR已经对不同淀粉样原纤维的结构产生了复杂的见解。这些研究揭示了通常符合交叉β淀粉样蛋白模式的多种多态性结构。本章简要概述了在蛋白质聚集领域获得的信息，特别关注淀粉样蛋白。
