Item type |
学術雑誌論文 / Journal Article(1) |
公開日 |
2017-10-03 |
タイトル |
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タイトル |
High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin |
言語 |
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言語 |
eng |
資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
ID登録 |
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ID登録 |
10.24517/00011001 |
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ID登録タイプ |
JaLC |
著者 |
Shibata, Mikihiro
Yamashita, Hayato
Uchihashi, Takayuki
Kandori, Hideki
Ando, Toshio
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著者別表示 |
柴田, 幹大
内橋, 貴之
安藤, 敏夫
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提供者所属 |
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内容記述タイプ |
Other |
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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 |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
1748-3387 |
NCID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA12163154 |
DOI |
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関連タイプ |
isVersionOf |
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識別子タイプ |
DOI |
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関連識別子 |
10.1038/nnano.2010.7 |
出版者 |
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出版者 |
Nature Publishing Group |
抄録 |
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内容記述タイプ |
Abstract |
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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 |
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出版タイプ |
AM |
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出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |