Yet another polymorph of α-synuclein: solid-state sequential assignments
Yet another polymorph of α-synuclein: solid-state sequential assignments
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DOI：
10.1007/s12104-013-9526-y
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发表时间：
2014-10-01
影响因子：
0.9
通讯作者：
Boeckmann, Anja
中科院分区：
文献类型：
--
作者：
Gath, Julia;Bousset, Luc;Boeckmann, Anja
帕金森氏病是一种神经性人类蛋白质病，由高分子量的蛋白质聚集体聚集引起。α-突触核蛋白是这些富含β-折叠的纤维状不可溶组件的主要成分，以淀粉样蛋白的形式沉积。虽然到目前为止还没有可用的原子分辨结构，但通过固体核磁共振可以表征淀粉样蛋白的结构。α-突触核蛋白，就像许多其他与病理相关的纤维形成蛋白一样，可以形成许多不同的多晶型，有时很难以纯形式获得。在这里，我们描述了一种多晶型的化学位移和二级结构分析，该多晶型也主要采用β-折叠构象，其纤维核心的残基范围从38到94。此外，来自N-末端的残基15-20被发现是刚性有序β-折叠的一部分。化学位移与我们之前指定的多晶型有很大的不同。
Parkinson's disease is a neurological human proteinopathy, which is caused by the accumulation of protein aggregates of high molecular mass. alpha-Synuclein is a major component of these fibrillar, beta-sheet rich, insoluble assemblies and is deposited in the form of amyloids. Structural characterization of amyloids is possible by solid-state NMR, although no atomic-resolution structure is available as of today. alpha-Synuclein, as many other pathology-related fibril-forming proteins, can form a number of different polymorphs that are sometimes tricky to obtain in pure form. Here, we describe the chemical shifts and secondary structure analysis of a polymorph that also adopts mainly beta-sheet conformation, with a fibrillar core ranging from residues 38 to 94. In addition, residues 15-20 from the N-terminus found to be part of a rigid ordered beta-sheet. The chemical shifts differ substantially from the polymorph we previously assigned.