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Journal of Electron Microscopy Advance Access published online on August 17, 2006
Journal of Electron Microscopy, 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
Received December 27, 2005
Accepted July 7, 2006

Full-length Paper

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

Yukihiro Sugiyama 1, Yuji Inoue 2, Eiro Muneyuki 3, Hajime Haneda 4, and Masayuki Fujimoto 1 *

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

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


  Abstract

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 {beta}-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 {beta}-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.
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