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

Ryo Tosaka, Hideaki Yamamoto, Iwao Ohdomari, Takanobu Watanabe

研究成果: Article

33 引用 (Scopus)

抜粋

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.

元の言語English
ページ(範囲)9950-9955
ページ数6
ジャーナルLangmuir
26
発行部数12
DOI
出版物ステータスPublished - 2010 6 15

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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