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Allostery without conformational change. A plausible model.

A Cooper, D T Dryden

    European Biophysics Journal : EBJ
    |January 1, 1984
    PubMed
    Summary
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    Ligand binding can alter protein dynamics to enable allosteric communication without changing protein shape. This dynamic allostery, driven by entropy, offers new insights into protein function and evolution.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Computational Biology

    Background:

    • Allosteric regulation is crucial for biological processes.
    • Traditional models focus on conformational changes for allostery.
    • The role of protein dynamics in allosteric communication is less understood.

    Purpose of the Study:

    • To present a general model for ligand-induced dynamic allostery.
    • To explore how changes in protein dynamics can mediate communication between binding sites.
    • To investigate the thermodynamic basis and potential magnitude of dynamic allosteric effects.

    Main Methods:

    • Theoretical analysis using statistical thermodynamics of ligand binding.
    • Modeling changes in macromolecular thermal fluctuations (frequencies and amplitudes).

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  • Derivation of expressions to calculate dynamic allosteric interactions from experimental data.

    • Main Results:

    • Ligand binding can induce allosteric communication via altered protein dynamics, even without conformational changes.
    • Cooperative interaction free energies of several kJ/mol can arise from these dynamic effects.
    • Dynamic allostery is primarily an entropy-driven effect involving various motional modes.

    Conclusions:

    • Proteins may exploit thermal fluctuations for functional advantages beyond static conformations.
    • Dynamic allostery provides a new mechanism for long-range communication in biological macromolecules.
    • This model offers a framework for quantifying allosteric effects based on dynamic properties.