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Structural analysis of human α-synuclein within amyloid fibrils by small-angle scattering
https://repo.qst.go.jp/records/77259
https://repo.qst.go.jp/records/772597dc6ca86-01c3-4c35-ad90-8d4741cf1e76
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2019-09-17 | |||||
| タイトル | ||||||
| タイトル | Structural analysis of human α-synuclein within amyloid fibrils by small-angle scattering | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference object | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Fujiwara, Satoru
× Fujiwara, Satoru× Matsuo, Tatsuhito× Sugimoto, Yasunobu× Fujiwara, Satoru× Matsuo, Tatsuhito |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Formation of amyloid fibrils of α-synuclein αSyn) is closely related to the pathogenesis of Parkinson's disease. Structural analysis of amyloid fibrils is important for elucidation of the mechanism of the fibril formation, and thus elucidation of the mechanism of the pathogenesis. Here we characterize the structure of amyloid fibrils of αSyn by small-angle X-ray and neutron scattering (SAXS and SANS), in particular, the structure of αSyn within fibrils. In addition to the information on the shape and the hydration structure of fibrils obtained from the combined analysis of SAXS and SANS, the information on the structure of individual αSyn within fibrils was obtained using the new SANS method. Comparison with the structure of αSyn in the monomeric state is discussed. | |||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 第57回日本生物物理学会年会 | |||||
| 発表年月日 | ||||||
| 日付 | 2019-09-24 | |||||
| 日付タイプ | Issued | |||||
