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Water near intracellular surfaces.

V A Parsegian, D C Rau

    The Journal of Cell Biology
    |July 1, 1984
    PubMed
    Summary

    Water molecules near soluble surfaces exert a hydration force. Specific molecular attractions are stronger than water interactions, explaining biochemical specificity.

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    Area of Science:

    • Biophysics
    • Molecular Biology
    • Physical Chemistry

    Background:

    • Water molecules exhibit altered behavior near soluble molecular surfaces.
    • Displacing this bound water requires significant energy, described as a hydration force.
    • Specific molecular interactions, like in ligand binding, suggest surface attractions outweigh water interactions.

    Purpose of the Study:

    • To investigate the role of water in molecular interactions.
    • To elucidate the mechanism behind the specificity of biochemical associations.
    • To explore the relationship between surface structure, hydration, and binding energy.

    Main Methods:

    • Analysis of hydration forces as a function of molecular separation.
    • Thermodynamic considerations of water displacement energetics.
    • Examination of protein-protein versus protein-water interaction competition.

    Main Results:

    • Water is perturbed within angstroms of soluble molecular surfaces.
    • A hydration force, exponentially dependent on separation, quantifies water displacement work.
    • Specific molecular associations are energetically favored over interactions with water.
    • Protein-water interactions compete with and influence protein-protein binding specificity.

    Conclusions:

    • Surface hydration and water displacement energetics are key to the specificity of intracellular associations.
    • Biochemical specificity arises from a balance between molecular surface attractions and competing protein-water interactions.
    • Minor alterations in molecular surface structure can significantly impact hydrated surface contact energy.

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