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Interaction between proteins localized in membranes.

B Grasberger, A P Minton, C DeLisi

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1986
    PubMed
    Summary
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    High concentrations of membrane proteins dramatically increase self-association likelihood. This excluded volume effect significantly enhances dimer and oligomer formation, impacting cellular events and protein assembly.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Membrane Biology

    Background:

    • Protein self-association in membranes is crucial for cellular functions.
    • High protein concentrations can influence molecular interactions through excluded volume effects.
    • Understanding these effects is key to deciphering membrane protein behavior.

    Purpose of the Study:

    • To develop a conceptual framework for assessing the impact of excluded volume effects on membrane protein self-association.
    • To quantify how high protein concentrations and preorientation influence protein complex formation.

    Main Methods:

    • Developed a theoretical model to calculate the effects of protein concentration, dimensions, tilt, and vertical movement.
    • Used plausible values for membrane protein concentrations and physical parameters.

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    Main Results:

    • Excluded volume effects and preorientation can increase the likelihood of dimer formation by 10^6-fold compared to free monomers.
    • These factors lead to many orders of magnitude greater likelihood for forming trimers and higher-order oligomers.

    Conclusions:

    • Excluded volume effects are a major driver of membrane protein self-association.
    • Findings have implications for membrane protein assembly, function, and the formation of membrane lesions.
    • The study provides insights into receptor-mediated cellular signaling.