Volume 5, Issue 18 pp. 2077-2084
Full Paper

A Self-Assembled Protein Nanotube with High Aspect Ratio

Frederico F. Miranda

Frederico F. Miranda

Protein Design Laboratory Yokohama City University 1-7-29 Suehiro-cho Tsurumi-ku

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Kenji Iwasaki

Kenji Iwasaki

Laboratory of Protein Synthesis and Expression Institute for Protein Research, Osaka University Suita, Osaka, Japan and CREST Japan Science and Technology Agency 4-1-8 Honcho, Kawaguchi, Saitama, 332-0012 (Japan)

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Satoko Akashi

Satoko Akashi

Structural Biology Laboratory Yokohama City University 1-7-29 Suehiro-cho Tsurumi-ku Yokohama, Kanagawa, 230-0045 (Japan)

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Koji Sumitomo

Koji Sumitomo

NTT Basic Research Laboratories 3-1 Morinosato-Wakamiya, Atsugi Kanagawa 243-0198 (Japan)

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Mime Kobayashi

Mime Kobayashi

Graduate School of Materials Science Nara Institute of Science and Technology 8916-5 Takayama, Ikoma, Nara 630-0192 (Japan)

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Ichiro Yamashita

Ichiro Yamashita

CREST, Japan Science and Technology Agency 4-1-8 Honcho, Kawaguchi Saitama, 332-0012 (Japan)

Graduate School of Materials Science Nara Institute of Science and Technology 8916-5 Takayama, Ikoma, Nara 630-0192 (Japan)

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Jeremy R. H. Tame

Corresponding Author

Jeremy R. H. Tame

Protein Design Laboratory Yokohama City University 1-7-29 Suehiro-cho Tsurumi-ku

Jeremy R. H. Tame, Protein Design Laboratory Yokohama City University 1-7-29 Suehiro-cho Tsurumi-ku.

Jonathan G. Heddle, Global Edge Institute Tokyo Institute of Technology 4259 S2-17, Nagatsuda, Midori-ku Yokohama, Kanagawa 226-8501 (Japan).

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Jonathan G. Heddle

Corresponding Author

Jonathan G. Heddle

Global Edge Institute Tokyo Institute of Technology 4259 S2-17, Nagatsuda, Midori-ku Yokohama, Kanagawa 226-8501 (Japan)

Jeremy R. H. Tame, Protein Design Laboratory Yokohama City University 1-7-29 Suehiro-cho Tsurumi-ku.

Jonathan G. Heddle, Global Edge Institute Tokyo Institute of Technology 4259 S2-17, Nagatsuda, Midori-ku Yokohama, Kanagawa 226-8501 (Japan).

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First published: 14 September 2009
Citations: 72

Abstract

Production of a self-assembled protein nanotube achieved through engineering of the 11mer ring protein trp RNA-binding attenuation protein is described. The produced mutant protein is able to stack in solution to produce an extremely narrow, uniform nanotube apparently stabilized by a mixture of disulfide bonds and hydrophobic interactions. Assembly is reversible and the length of tube can potentially be controlled. Large quantities of hollow tubes 8.5 nm in overall diameter with lengths varying from 7 nm to over 1 µm are produced. The structure is analyzed using transmission electron microscopy, atomic force microscopy, mass spectrometry, and single-particle analysis and it is found that component rings stack in a head-to-head fashion. The internal diameter of the tube is 2.5 nm, and the amino acid residues lining the central cavity can be mutated, raising the possibility that the tube can be filled with a variety of conducting or semiconducting materials.

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