Visualization of intrinsically disordered proteins by high-speed atomic force microscopy |
| |
| Affiliation: | 1. Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa 920-1192, Japan;2. Department of Physics, Kanazawa University, Kanazawa 920-1192, Japan;3. Graduate School of Natural Science & Technology, Kanazawa University, Kanazawa 920-1192, Japan;1. Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa 920-1192, Japan;2. Department of Life Sciences, Prefectural University of Hiroshima, 562 Nanatsuka, Shobara, Hiroshima 727-0023, Japan;3. Department of Physics, Kanazawa University, Kanazawa 920-1192, Japan;1. Department of Applied Physics, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan;2. Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan;3. Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, Aichi 444-8787, Japan;4. Department of Physics, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8602, Japan |
| |
| Abstract: | High-speed atomic force microscopy (HS-AFM) is a powerful tool established 13 years ago. This methodology can capture individual protein molecules carrying out functional activities under near-physiological conditions, without chemical labeling, at 2–3 nm lateral and ∼0.1 nm vertical spatial resolution, and at sub-100 ms temporal resolution. Although most biological HS-AFM studies thus far target structured proteins, HS-AFM is also ideally suited to study the dynamics of intrinsically disordered proteins. Here we review some of the dynamic structures and processes of intrinsically disordered proteins that have been unveiled by HS-AFM imaging. |
| |
| Keywords: | AFM" },{" #name" :" keyword" ," $" :{" id" :" pc_FvmNMkbSA8" }," $$" :[{" #name" :" text" ," _" :" atomic force microscopy |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
