Remaining structures at the N‐ and C‐terminal regions of alpha‐synuclein accurately elucidated by amide‐proton exchange NMR with fitting. Issue 22 (7th October 2013)

• Record Type: Journal Article
• Authors: Okazaki, Honoka; Ohori, Yuka; Komoto, Masaya; Lee, Young-Ho; Goto, Yuji; Tochio, Naoya; Nishimura, Chiaki
• Is Part Of: FEBS letters. Volume 587:Issue 22(2013)
• Page Start: 3709
• Page End: 3714
• Publication Date: 2013-10-07
• Subjects: Alpha-synuclein -- Unfolded protein -- NMR -- Protein folding -- Amide proton exchange; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.09.039
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract : The CLEANEX‐PM methodology is useful to analyze the residual structure. Accurate information was acquired by linear fitting with data points. The EX2 regime of the proton exchange was confirmed by α‐synuclein system. Residual structure existed at the N‐terminal and C‐terminal regions. The middle part including NAC region is not completely protected.