Violation of the fluctuation-dissipation theorem in a protein system

Kumiko Hayashi, Mitsunori Takano

    Research output: Contribution to journalArticle

    20 Citations (Scopus)

    Abstract

    We report the results of molecular dynamics simulations of the protein myosin carried out with an elastic network model. Quenching the system, we observe glassy behavior of a density correlation function and a density response function that are often investigated in structure glasses and spin glasses. In the equilibrium, the fluctuation-response relation, a representative relation of the fluctuation-dissipation theorem, holds that the ratio of the density correlation function to the density response function is equal to the temperature of the environment. We show that, in the quenched system that we study, this relation can be violated. In the case that this relation does not hold, this ratio can be regarded as an effective temperature. We find that this effective temperature of myosin is higher than the temperature of the environment. We discuss the relation between this effective temperature and energy transduction that occurs after ATP hydrolysis in the myosin molecule.

    Original languageEnglish
    Pages (from-to)895-901
    Number of pages7
    JournalBiophysical Journal
    Volume93
    Issue number3
    DOIs
    Publication statusPublished - 2007 Aug

    Fingerprint

    Myosins
    Temperature
    Proteins
    Glass
    Molecular Dynamics Simulation
    Hydrolysis
    Adenosine Triphosphate

    ASJC Scopus subject areas

    • Biophysics

    Cite this

    Violation of the fluctuation-dissipation theorem in a protein system. / Hayashi, Kumiko; Takano, Mitsunori.

    In: Biophysical Journal, Vol. 93, No. 3, 08.2007, p. 895-901.

    Research output: Contribution to journalArticle

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