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

    29 引用 (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.

    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

    Fingerprint

    Molecular Dynamics Simulation
    Silicon Dioxide
    Adsorption
    Molecular dynamics
    Silica
    molecular dynamics
    silicon dioxide
    proteins
    Proteins
    adsorption
    Computer simulation
    simulation
    Large Ribosome Subunits
    Coulomb interactions
    Static Electricity
    affinity
    ribosomal protein L2
    flexibility
    electrostatics
    interactions

    ASJC Scopus subject areas

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

    これを引用

    Adsorption mechanism of ribosomal protein L2 onto a silica surface : A molecular dynamics simulation study. / Tosaka, Ryo; Yamamoto, Hideaki; Ohdomari, Iwao; Watanabe, Takanobu.

    :: Langmuir, 巻 26, 番号 12, 15.06.2010, p. 9950-9955.

    研究成果: Article

    Tosaka, Ryo ; Yamamoto, Hideaki ; Ohdomari, Iwao ; Watanabe, Takanobu. / Adsorption mechanism of ribosomal protein L2 onto a silica surface : A molecular dynamics simulation study. :: Langmuir. 2010 ; 巻 26, 番号 12. pp. 9950-9955.
    @article{8314321150514ac2b9798c47ab08c934,
    title = "Adsorption mechanism of ribosomal protein L2 onto a silica surface: A molecular dynamics simulation study",
    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.",
    author = "Ryo Tosaka and Hideaki Yamamoto and Iwao Ohdomari and Takanobu Watanabe",
    year = "2010",
    month = "6",
    day = "15",
    doi = "10.1021/la1004352",
    language = "English",
    volume = "26",
    pages = "9950--9955",
    journal = "Langmuir",
    issn = "0743-7463",
    publisher = "American Chemical Society",
    number = "12",

    }

    TY - JOUR

    T1 - Adsorption mechanism of ribosomal protein L2 onto a silica surface

    T2 - A molecular dynamics simulation study

    AU - Tosaka, Ryo

    AU - Yamamoto, Hideaki

    AU - Ohdomari, Iwao

    AU - Watanabe, Takanobu

    PY - 2010/6/15

    Y1 - 2010/6/15

    N2 - 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.

    AB - 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.

    UR - http://www.scopus.com/inward/record.url?scp=77956074837&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=77956074837&partnerID=8YFLogxK

    U2 - 10.1021/la1004352

    DO - 10.1021/la1004352

    M3 - Article

    C2 - 20429542

    AN - SCOPUS:77956074837

    VL - 26

    SP - 9950

    EP - 9955

    JO - Langmuir

    JF - Langmuir

    SN - 0743-7463

    IS - 12

    ER -