کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1936990 | 1050706 | 2007 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of α-synuclein
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 363, Issue 3, 23 November 2007, Pages 795–799
Journal: Biochemical and Biophysical Research Communications - Volume 363, Issue 3, 23 November 2007, Pages 795–799
نویسندگان
Hiroaki Sasakawa, Eri Sakata, Yoshiki Yamaguchi, Masami Masuda, Tetsuya Mori, Eiji Kurimoto, Takeshi Iguchi, Shin-ichi Hisanaga, Takeshi Iwatsubo, Masato Hasegawa, Koichi Kato,