Solid-state NMR sequential assignments of α-synuclein

被引：57

作者：

Gath, Julia ^{[1
]}

Habenstein, Birgit ^{[2
]}

Bousset, Luc ^{[3
]}

Melki, Ronald ^{[3
]}

Meier, Beat H. ^{[1
]}

Boeckmann, Anja ^{[2
]}

机构：

[1] ETH, CH-8093 Zurich, Switzerland

[2] Univ Lyon 1, Inst Biol & Chim Prot, UMR 5086, CNRS, F-69367 Lyon, France

[3] CNRS, Lab Enzymol & Biochim Struct, UPR 3082, F-91198 Gif Sur Yvette, France

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2012年 / 6卷 / 01期

基金：

瑞士国家科学基金会;

关键词：

alpha-Synuclein; Fibrils; Solid-state NMR; Assignments; Secondary structure; AMYLOID FIBRILS; SECONDARY STRUCTURE; CORE STRUCTURE; WILD-TYPE; SPECTROSCOPY; REVEALS; WATER;

D O I：

10.1007/s12104-011-9324-3

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Parkinson's disease is amongst the most frequent and most devastating neurodegenerative diseases. It is tightly associated with the assembly of proteins into high-molecular weight protein species, which propagate between neurons in the central nervous system. The principal protein involved in this process is a-synuclein which is a structural component of the Lewy bodies observed in diseased brain. We here present the solid-state NMR sequential assignments of a new fibrillar form of this protein, the first one with a well-ordered and rigid N-terminal part.

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页码：51 / 55

页数：5

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