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Thermodynamic fluctuations in protein molecules.

A Cooper

    Proceedings of the National Academy of Sciences of the United States of America
    |August 1, 1976
    PubMed
    Summary

    Thermodynamic fluctuations in single globular proteins explain apparent contradictions in their physical nature. These molecular dynamics reconcile static and dynamic views, offering a unified understanding of macromolecular behavior.

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    Area of Science:

    • Biophysics
    • Physical Chemistry
    • Molecular Biology

    Background:

    • Conflicting views exist regarding the physical nature of globular proteins and macromolecules.
    • Understanding macromolecular behavior requires reconciling dynamic and static perspectives.

    Purpose of the Study:

    • To reconcile apparently conflicting views on the physical nature of globular proteins.
    • To explain macromolecular behavior through the lens of thermodynamic fluctuations.

    Main Methods:

    • Consideration of inherent thermodynamic fluctuations in microscopic systems.
    • Analysis of discrete protein molecules and their stochastic properties.
    • Comparison with time-averaged studies of protein ensembles.

    Main Results:

    • Discrete protein molecules exhibit significant fluctuations in thermodynamic and stochastic properties.
    • These fluctuations are reconcilable with time-averaged ensemble studies.
    • A unified view emerges that incorporates both dynamic fluctuations and average structural properties.

    Conclusions:

    • Thermodynamic fluctuations are key to understanding the physical nature of globular proteins.
    • The study reconciles dynamic, stochastic behavior of single molecules with static, averaged properties of ensembles.
    • This provides a more comprehensive model for macromolecular behavior.

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