High-speed atomic force microscopy for studying the dynamic behavior of protein molecules at work

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作者
Ando, Toshio [1 ,2 ,3 ]
Uchihashi, Takayuki [1 ,3 ]
Kodera, Noriyuki [1 ]
Miyagi, Atsushi [1 ]
Nakakita, Ryo [1 ]
Yamashita, Hayato [1 ]
Sakashita, Mitsuru [1 ]
机构
[1] Department of Physics, Faculty of Science, Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan
[2] Frontier Science Research Organization, Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan
[3] JST/CREST, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan
关键词
In the quest for the mechanism of protein functions; various key techniques and instruments have been developed. This is an era when scrutinizing a certain protein from various angles is becoming possible through combined knowledge of its structure and function. However; it is necessary to link these different aspects of a protein along a time axis; but no technology is available for tracing a protein in action; at high spatial and temporal resolutions. Atomic force microscopy made it possible for the first time to view a nanometer-scale world in an aqueous environment. In 2001; we developed the first-generation high-speed atomic force microscope (AFM) that could capture moving protein molecules on video at 80 ms/frame. Since then; we have been carrying out various efforts to increase its scan rate as well as to substantially reduce tip-sample interaction force. The reduction in this force is a key to making the high-speed AFM practically useful in life sciences. Various new techniques and devices developed in the past four years have brought the AFM to its second-generation stage. It can now capture weakly interacting protein molecules successively without disturbing their physiological function. Here; we report our efforts made over the past four years; the present capacity of the high-speed AFM; and our preliminary work on the next generation of the instrument. © 2006 The Japan Society of Applied Physics;
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页码:1897 / 1903
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