Adsorption mechanism of ribosomal protein L2 onto a silica surface: A molecular dynamics simulation study

Ryo Tosaka*, Hideaki Yamamoto, Iwao Ohdomari, Takanobu Watanabe

*この研究の対応する著者

研究成果: Article査読

33 被引用数 (Scopus)

抄録

A large-scale molecular dynamics simulation was carried out in order to investigate the adsorption mechanism of ribosomal protein L2 (RPL2) onto a silica surface at various pH values. RPL2 is a constituent protein of the 50S large ribosomal subunit, and a recent experimental report showed that it adsorbs strongly to silica surfaces and that it can be used to immobilize proteins on silica surfaces. The simulation results show that RPL2, especially domains 1 (residues 1-60) and 3 (residues 203-273), adsorbed more tightly to the silica surface above pH 7. We found that a major driving force for the adsorption of RPL2 onto the silica surface is the electrostatic interaction and that the structural flexibility of domains 1 and 3 may further contribute to the high affinity.

本文言語English
ページ(範囲)9950-9955
ページ数6
ジャーナルLangmuir
26
12
DOI
出版ステータスPublished - 2010 6 15

ASJC Scopus subject areas

  • 材料科学(全般)
  • 凝縮系物理学
  • 表面および界面
  • 分光学
  • 電気化学

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