{"created":"2023-07-27T06:27:02.304925+00:00","id":11014,"links":{},"metadata":{"_buckets":{"deposit":"e76df06c-21f6-4432-beeb-0dea7b191783"},"_deposit":{"created_by":3,"id":"11014","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"11014"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00011014","sets":["4161:3020:3021"]},"author_link":["15800","2912","13404","2361","17049","16500","17048","98"],"item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2010-03-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"3","bibliographicPageEnd":"212","bibliographicPageStart":"208","bibliographicVolumeNumber":"5","bibliographic_titles":[{"bibliographic_title":"Nature Nanotechnology"}]}]},"item_4_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"柴田, 幹大"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"内橋, 貴之"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"安藤, 敏夫"}],"nameIdentifiers":[{},{}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"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.","subitem_description_type":"Abstract"}]},"item_4_description_5":{"attribute_name":"提供者所属","attribute_value_mlt":[{"subitem_description":"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","subitem_description_type":"Other"}]},"item_4_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00011001","subitem_identifier_reg_type":"JaLC"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Nature Publishing Group"}]},"item_4_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1038/nnano.2010.7","subitem_relation_type_select":"DOI"}}]},"item_4_source_id_11":{"attribute_name":"NCID","attribute_value_mlt":[{"subitem_source_identifier":"AA12163154","subitem_source_identifier_type":"NCID"}]},"item_4_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"1748-3387","subitem_source_identifier_type":"ISSN"}]},"item_4_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Shibata, Mikihiro"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"Yamashita, Hayato"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Uchihashi, Takayuki"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"Kandori, Hideki"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Ando, Toshio"}],"nameIdentifiers":[{},{},{},{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-10-03"}],"displaytype":"detail","filename":"SC-PR-ANDO-T-208.pdf","filesize":[{"value":"691.2 kB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"SC-PR-ANDO-T-208.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/11014/files/SC-PR-ANDO-T-208.pdf"},"version_id":"67fc6df5-971b-4ac6-98b1-2db92633f3a6"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin"}]},"item_type_id":"4","owner":"3","path":["3021"],"pubdate":{"attribute_name":"公開日","attribute_value":"2017-10-03"},"publish_date":"2017-10-03","publish_status":"0","recid":"11014","relation_version_is_last":true,"title":["High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin"],"weko_creator_id":"3","weko_shared_id":3},"updated":"2023-07-27T10:16:21.073376+00:00"}