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Journal of Electron Microscopy Advance Access originally published online on August 17, 2006
Journal of Electron Microscopy 2006 55(3):143-149; doi:10.1093/jmicro/dfl024
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© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Microscopy. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

AFM and TEM observations of {alpha}-helix to ß-sheet conformational change occurring on carbon nanotubes

Yukihiro Sugiyama1, Yuji Inoue2, Eiro Muneyuki3, Hajime Haneda4 and Masayuki Fujimoto1,*

1 Graduate School of Electronic Science and Technology, Shizuoka University 3-5-1 Jyouhoku, Hamamatsu, Shizuoka 432-8561
2 Chemical Resources Laboratory, Tokyo Institute of Technology 4259, Nagatsutacho, Yokohama 226-8503
3 Chuo University, Faculty of Science and Engineering, Department of Physics 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8501
4 Sensor Materials Center, National Institute for Materials Science 1-1 Namiki, Tsukuba, Ibaraki 305-0044, Japan

*To whom correspondence should be addressed. E-mail: fujimoto{at}cjr.shizuoka.ac.jp

Bacteriorhodopsin (BR), which is rich in {alpha}-helical structure, was spread onto water with single-wall carbon nanotubes (SCNTs). After a Langmuir trough was used to apply compressive surface pressure to maintain the {alpha}-helices monolayer of denatured BR, the composite films comprising {alpha}-helices and SCNTs were transferred horizontally onto substrates. Atomic force microscopy (AFM) and fluorescence microscopy observation suggested that {alpha}-helices in contact with SCNTs changed into ß-sheets. High-resolution transmission electron microscopy (HR-TEM) showed 0.54 nm periodicity characteristic of the turn of {alpha}-helical structure in the SCNTs-free {alpha}-helix monolayer region and showed the 0.70 nm periodicity of ß-sheet pleated structure in the region where SCNTs were covered with unfolded BR. Unique features of carbon nanotubes that trigger conformational changes of a protein were revealed.

Keywords     carbon nanotubes, protein, conformational change, AFM, HR-TEM

Received     27 December 2005, accepted 7 July 2006


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