Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting

被引：13
作者：
Okazaki, Honoka [1 ]
Ohori, Yuka [1 ]
Komoto, Masaya [1 ]
Lee, Young-Ho [2 ]
Goto, Yuji [2 ]
Tochio, Naoya [3 ]
Nishimura, Chiaki [1 ,2 ]
机构：
[1] Teikyo Heisei Univ, Fac Pharmaceut Sci, Nakano Ku, Tokyo 1648530, Japan
[2] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
[3] RIKEN, Yokohama Inst, Ctr Life Sci Technol, NMR Facil, Yokohama, Kanagawa 2300045, Japan
来源：
FEBS LETTERS | 2013年 / 587卷 / 22期
关键词：
Alpha-synuclein; Unfolded protein; NMR; Protein folding; Amide proton exchange; INTRINSICALLY DISORDERED PROTEIN; PARKINSONS-DISEASE; HYDROGEN-EXCHANGE; RESIDUAL STRUCTURE; AGGREGATION; DYNAMICS; BINDING; FIBRILLATION; TEMPERATURE; MECHANISM;
D O I：
10.1016/j.febslet.2013.09.039
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：3709 / 3714
页数：6
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