Mutual positional preference of IPMDH proteins for binding studied by coarse-grained molecular dynamics simulation

T. Ishioka, H. Yamada*, T. Miyakawa, R. Morikawa, S. Akanuma, A. Yamagishi, M. Takasu

*この研究の対応する著者

研究成果: Conference contribution

抄録

Proteins, which incorporate charged and hydrophobic amino acid residues, are useful as a material of nanotechnology. Among these proteins, IPMDH (3-isopropylmalate dehydrogenase), which has thermal stability, has potential as a material of nanofiber. In this study, we performed coarse-grained molecular dynamics simulation of IPMDH using MARTINI force fields, and we investigated the orientation for the binding of IPMDH. In simulation, we analyzed wild type of IPMDH and the mutated IPMDH proteins, where 13, 20, 27, 332, 335 and 338th amino acid residues are replaced by lysine residues which have positive charge and by glutamic acid residues which have negative charge. Since the binding of mutated IPMDH is advantageous compared with the binding of wild type for one orientation, we suggest that the Coulomb interaction for the binding of IPMDH is important.

本文言語English
ホスト出版物のタイトルInternational Conference of Computational Methods in Sciences and Engineering 2016, ICCMSE 2016
編集者Zacharoula Kalogiratou, Theodore E. Simos, Theodore Monovasilis, Theodore E. Simos, Theodore E. Simos
出版社American Institute of Physics Inc.
ISBN(電子版)9780735414549
DOI
出版ステータスPublished - 2016 12月 6
イベントInternational Conference of Computational Methods in Sciences and Engineering 2016, ICCMSE 2016 - Athens, Greece
継続期間: 2016 3月 172016 3月 20

出版物シリーズ

名前AIP Conference Proceedings
1790
ISSN(印刷版)0094-243X
ISSN(電子版)1551-7616

Other

OtherInternational Conference of Computational Methods in Sciences and Engineering 2016, ICCMSE 2016
国/地域Greece
CityAthens
Period16/3/1716/3/20

ASJC Scopus subject areas

  • 物理学および天文学(全般)

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