Piezoelectric allostery of protein

    Research output: Contribution to journalArticle

    7 Citations (Scopus)

    Abstract

    Allostery is indispensable for a protein to work, where a locally applied stimulus is transmitted to a distant part of the molecule. While the allostery due to chemical stimuli such as ligand binding has long been studied, the growing interest in mechanobiology prompts the study of the mechanically stimulated allostery, the physical mechanism of which has not been established. By molecular dynamics simulation of a motor protein myosin, we found that a locally applied mechanical stimulus induces electrostatic potential change at distant regions, just like the piezoelectricity. This novel allosteric mechanism, "piezoelectric allostery", should be of particularly high value for mechanosensor/transducer proteins.

    Original languageEnglish
    Article number012406
    JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
    Volume94
    Issue number1
    DOIs
    Publication statusPublished - 2016 Jul 13

    Fingerprint

    stimuli
    proteins
    Protein
    Mechanobiology
    Piezoelectricity
    myosins
    piezoelectricity
    Myosin
    Transducer
    Electrostatics
    Molecular Dynamics Simulation
    transducers
    Molecules
    electrostatics
    molecular dynamics
    ligands
    molecules
    simulation

    ASJC Scopus subject areas

    • Condensed Matter Physics
    • Statistical and Nonlinear Physics
    • Statistics and Probability

    Cite this

    Piezoelectric allostery of protein. / Ohnuki, Jun; Sato, Takato; Takano, Mitsunori.

    In: Physical Review E - Statistical, Nonlinear, and Soft Matter Physics, Vol. 94, No. 1, 012406, 13.07.2016.

    Research output: Contribution to journalArticle

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