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Revealing molecular-level surface structure of amyloid fibrils in liquid by means of frequency modulation atomic force microscopy
https://doi.org/10.24517/00039984
https://doi.org/10.24517/000399840a776120-ecc4-4957-9cef-c6c1774a8ed4
| 名前 / ファイル | ライセンス | アクション |
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FS-PR-FUKUMA-T-384010.pdf (118.9 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2017-10-06 | |||||||
| タイトル | ||||||||
| タイトル | Revealing molecular-level surface structure of amyloid fibrils in liquid by means of frequency modulation atomic force microscopy | |||||||
| 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_6501 | |||||||
| 資源タイプ | journal article | |||||||
| ID登録 | ||||||||
| ID登録 | 10.24517/00039984 | |||||||
| ID登録タイプ | JaLC | |||||||
| 著者 |
Fukuma, Takeshi
× Fukuma, Takeshi× Mostaert, Anika S.× Serpell, Louise C.× Jarvis, Suzanne P. |
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| 著者別表示 |
福間, 剛士
× 福間, 剛士
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| 提供者所属 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | 金沢大学フロンティアサイエンス機構 | |||||||
| 書誌情報 |
Nanotechnology 巻 19, 号 38, p. 384010, 発行日 2008-09-24 |
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| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0957-4484 | |||||||
| NCID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AA10863359 | |||||||
| DOI | ||||||||
| 関連タイプ | isIdenticalTo | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | 10.1088/0957-4484/19/38/384010 | |||||||
| 出版者 | ||||||||
| 出版者 | Institute of Physics | |||||||
| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | We have investigated the surface structure of islet amyloid polypeptide (IAPP) fibrils and α-synuclein protofibrils in liquid by means of frequency modulation atomic force microscopy (FM-AFM). Ångström- resolution FM-AFM imaging of isolated macromolecules in liquid is demonstrated for the first time. Individual β-strands aligned perpendicular to the fibril axis with a spacing of 0.5 nm are resolved in FM-AFM images, which confirms cross-β structure of IAPP fibrils in real space. FM-AFM images also reveal the existence of 4 nm periodic domains along the axis of IAPP fibrils. Stripe features with 0.5 nm spacing are also found in images of α-synuclein protofibrils. However, in contrast to the case for IAPP fibrils, the stripes are oriented 30° from the axis, suggesting the possibility of β-strand alignment in protofibrils different from that in mature fibrils or the regular arrangement of thioflavin T molecules present during the fibril preparation aligned at the surface of the protofibrils. © IOP Publishing Ltd. | |||||||
| 著者版フラグ | ||||||||
| 出版タイプ | VoR | |||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||
