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

Ryo Tosaka, Hideaki Yamamoto, Iwao Ohdomari, Takanobu Watanabe

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)9950-9955
Number of pages6
JournalLangmuir
Volume26
Issue number12
DOIs
Publication statusPublished - 2010 Jun 15

ASJC Scopus subject areas

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

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