Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting
Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting
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DOI：
10.1016/j.febslet.2013.09.039
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发表时间：
2013-11-15
期刊：
影响因子：
3.5
通讯作者：
Nishimura, Chiaki
中科院分区：
文献类型：
--
作者：
Okazaki, Honoka;Ohori, Yuka;Nishimura, Chiaki
通过CLEANEX-PM方法分析生理条件下的α -突触核蛋白，该方法可以在毫秒尺度上监测酰胺-质子交换。k（ex）和[OH]之间的关系与斜率1呈线性相关，表明EX2状态。在N端和c端有明显的残余结构。c端结构比n端结构更稳定。包括NAC地区在内的中部地区并没有得到完全保护。在不同的pH值和混合时间条件下获得的数据，然后进行线性拟合，可以得到关于残余结构的准确信息。(C) 2013年欧洲生化学会联合会。Elsevier B.V.版权所有。
Alpha-synuclein is analyzed in physiological conditions by CLEANEX-PM methodology, in which the amide-proton exchange can be monitored at millisecond scale. The relationship between k(ex) and [OH] is confirmed as a linear correlation with slope 1, indicating EX2 regime. There are significant residual structures at the N- and C-terminal regions. The structure at the C-terminal region is more stable than that of the N-terminal region. The middle part including NAC region is not completely protected. The data acquired at various pH and mixing time conditions followed by linear fitting give accurate information about residual structures. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.