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Viscosity scaling and protein dynamics.

W Doster

    Biophysical Chemistry
    |March 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Protein internal motions slow down as solvent viscosity increases, influenced by protein flexibility and solvent interactions. This dynamic friction model explains viscosity-dependent molecular oxygen binding in myoglobin.

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    Area of Science:

    • Biophysics
    • Protein Dynamics
    • Chemical Kinetics

    Background:

    • Protein internal molecular motions are crucial for biological function.
    • Solvent viscosity can influence protein dynamics and reaction rates.

    Purpose of the Study:

    • To investigate the relationship between protein internal molecular motion rates and external solvent viscosity.
    • To develop a theoretical model explaining the observed viscosity dependence.
    • To apply the model to understand oxygen binding in myoglobin.

    Main Methods:

    • Analysis of scaling laws for protein internal motion rates with solvent viscosity.
    • Development of a dynamic friction model incorporating protein structural fluctuations.
    • Application of a generalized Langevin equation and fluctuation-dissipation theorem.

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  • Decomposition of fluctuation spectrum into solvent-dependent and independent components.

    • Main Results:

    • Protein internal motion rates exhibit an inverse power-law dependence on solvent viscosity.
    • A flexible protein structure, partially controlled by solvent, explains the observed scaling.
    • The derived dynamic friction model successfully explains viscosity-dependent oxygen binding rates in myoglobin.

    Conclusions:

    • Protein dynamics are significantly influenced by solvent viscosity through a dynamic friction mechanism.
    • Structural fluctuations within proteins, coupled with solvent interactions, dictate reaction dynamics.
    • The model provides insights into the molecular mechanisms of ligand binding in proteins like myoglobin.