Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1936990 | Biochemical and Biophysical Research Communications | 2007 | 5 Pages |
Abstract
Although biological importance of intrinsically disordered proteins is becoming recognized, NMR analyses of this class of proteins remain as tasks with more challenge because of poor chemical shift dispersion. It is expected that ultra-high field NMR spectroscopy offers improved resolution to cope with this difficulty. Here, we report an ultra-high field NMR study of α-synuclein, an intrinsically disordered protein identified as the major component of the Lewy bodies. Based on NMR spectral data collected at a 920 MHz proton frequency, we performed epitope mapping of an anti-α-synuclein monoclonal antibody, and furthermore, characterized conformational effects of phosphorylation at Ser129 of α-synuclein.
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Authors
Hiroaki Sasakawa, Eri Sakata, Yoshiki Yamaguchi, Masami Masuda, Tetsuya Mori, Eiji Kurimoto, Takeshi Iguchi, Shin-ichi Hisanaga, Takeshi Iwatsubo, Masato Hasegawa, Koichi Kato,