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High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin
https://doi.org/10.24517/00011001
https://doi.org/10.24517/000110010dfb4bad-ff92-4d64-8ad4-c9daf2e82f81
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-ANDO-T-208.pdf (691.2 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2017-10-03 | |||||||||||
| タイトル | ||||||||||||
| タイトル | High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin | |||||||||||
| 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 | 10.24517/00011001 | |||||||||||
| ID登録タイプ | JaLC | |||||||||||
| 著者 |
Shibata, Mikihiro
× Shibata, Mikihiro× Yamashita, Hayato× Uchihashi, Takayuki× Kandori, Hideki× Ando, Toshio |
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| 著者別表示 |
柴田, 幹大
× 柴田, 幹大
× 内橋, 貴之
× 安藤, 敏夫
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| 提供者所属 | ||||||||||||
| 内容記述タイプ | Other | |||||||||||
| 内容記述 | 金沢大学ナノ生命科学研究所 / 金沢大学理工研究域数物科学系 | |||||||||||
| 書誌情報 |
Nature Nanotechnology 巻 5, 号 3, p. 208-212, 発行日 2010-03-01 |
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| ISSN | ||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||
| 収録物識別子 | 1748-3387 | |||||||||||
| NCID | ||||||||||||
| 収録物識別子タイプ | NCID | |||||||||||
| 収録物識別子 | AA12163154 | |||||||||||
| DOI | ||||||||||||
| 関連タイプ | isVersionOf | |||||||||||
| 識別子タイプ | DOI | |||||||||||
| 関連識別子 | 10.1038/nnano.2010.7 | |||||||||||
| 出版者 | ||||||||||||
| 出版者 | Nature Publishing Group | |||||||||||
| 抄録 | ||||||||||||
| 内容記述タイプ | Abstract | |||||||||||
| 内容記述 | Dynamic changes in protein conformation in response to external stimuli are important in biological processes, but it has proved difficult to directly visualize such structural changes under physiological conditions1-10. Here, we show that high-speed atomic force microscopy7 can be used to visualize dynamic changes in stimulated proteins. High-resolution movies of a light-driven proton pump, bacteriorhodopsin, reveal that, upon illumination, a cytoplasmic portion of each bacteriorhodopsin monomer is brought into contact with adjacent trimers. The bacteriorhodopsin-bacteriorhodopsin11,12 interaction in the transiently formed assembly engenders both positive and negative cooperative effects in the decay kinetics as the initial bacteriorhodopsin recovers and, as a consequence, the turnover rate of the photocycle is maintained constant, on average, irrespective of the light intensity. These results confirm that high-resolution visualization is a powerful approach for studying elaborate biomolecular processes under realistic conditions. © 2010 Macmillan Publishers Limited. All rights reserved. | |||||||||||
| 著者版フラグ | ||||||||||||
| 出版タイプ | AM | |||||||||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||||||||
