@article{oai:kanazawa-u.repo.nii.ac.jp:00010906,
 author = {Ando, Toshio and Kodera, Noriyuki and 安藤, 敏夫 and 古寺, 哲幸},
 issue = {1},
 journal = {生物物理 = Biophys},
 month = {Jan},
 note = {Proteins are dynamic in nature and work at the single-molecule level. Reflecting this fact, single-molecule fluorescence microscopy has been widely exploited to understand how proteins operate. However, what we can observe thereby is the dynamic behaviour of individual fluorescent spots (each being emitted from a fluorophore attached to a selected locus of the molecule), not of the protein molecules themselves. The structure of proteins has been studied by electron microscopy, X-ray crystallography and NMR, but the obtained structures are essentially static. This long-standing problem prevailing throughout biological research has been recently overcome by the development of high-speed atomic force microscopy that enables simultaneous recording of the structure and dynamics of functioning biomolecules with high spatiotemporal resolution., 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 = {022--025},
 title = {高速原子間力顕微鏡によるタンパク質の動態撮影},
 volume = {51},
 year = {2011}
}