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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 |