Designing the Binding Surface of Proteins to Construct Nano-fibers

Y. Komatsu*, H. Yamada, M. Fukuda, T. Miyakawa, R. Morikawa, M. Takasu, S. Akanuma, A. Yamagishi, S. Kawamoto

*この研究の対応する著者

研究成果: Chapter

2 被引用数 (Scopus)

抄録

In the field of nanotechnology, a variety of applications have been anticipated. We have been trying to design nano-fibers using proteins while maintaining their native structures. We try to use Lac repressor two-helix protein (LARFH), sulerythrin, and 3-isopropylmalate dehydrogenase (IPMDH) as adaptors for constructing nano-fibers. By making use of the α-helices outside of respective proteins, we are trying to form binding site between proteins: two α-helices of one protein are designed to form four-helix bundle with two α-helices of another protein. In addition, by introducing mutations in amino acids at the binding sites, hydrophobic and electrostatic interactions can be modified. The fiber may be produced upon mixing the two kinds of proteins. By umbrella sampling simulation, we have found that in the combination of LARFH-/-LARFH, hydrophobic interaction is enhanced in wild type, and electrostatic interaction is enhanced in variant. We also found high stability of IPMDH-/-IPMDH.

本文言語English
ホスト出版物のタイトルProgress in Theoretical Chemistry and Physics
出版社Springer Nature
ページ555-567
ページ数13
DOI
出版ステータスPublished - 2012
外部発表はい

出版物シリーズ

名前Progress in Theoretical Chemistry and Physics
26
ISSN(印刷版)1567-7354
ISSN(電子版)2215-0129

ASJC Scopus subject areas

  • 化学 (全般)
  • 物理学および天文学(全般)
  • 生化学、遺伝学、分子生物学(その他)

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