@article{oai:kanazawa-u.repo.nii.ac.jp:00011014,
 author = {柴田, 幹大 and 内橋, 貴之 and 安藤, 敏夫 and Shibata, Mikihiro and Yamashita, Hayato and Uchihashi, Takayuki and Kandori, Hideki and Ando, Toshio},
 issue = {3},
 journal = {Nature Nanotechnology},
 month = {Mar},
 note = {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., 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},
 pages = {208--212},
 title = {High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin},
 volume = {5},
 year = {2010}
}