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Study of ethanol-lysozyme interactions using neutron diffraction.

M S Lehmann, S A Mason, G J McIntyre

    Biochemistry
    |October 8, 1985
    PubMed
    Summary
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    Neutron diffraction revealed how deuterated ethanol interacts with lysozyme crystals. Ethanol binds primarily to hydrophobic sites without altering lysozyme structure, suggesting dehydration causes denaturation at high concentrations.

    Area of Science:

    • Structural biology
    • Biophysics
    • Crystallography

    Background:

    • Lysozyme is a key model protein for studying denaturation.
    • Alcohol interactions with proteins are crucial for understanding biological processes and drug formulation.
    • Previous studies have investigated protein-alcohol interactions using various techniques.

    Purpose of the Study:

    • To elucidate the specific binding sites and interactions of ethanol with lysozyme.
    • To investigate the effect of ethanol on lysozyme's molecular structure and dynamics.
    • To propose a mechanism for alcohol-induced protein denaturation.

    Main Methods:

    • Single-crystal neutron diffraction was employed.
    • Triclinic hen egg white lysozyme crystals were soaked in 25% (v/v) deuterated ethanol solutions.

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  • Structure refinement was performed to a resolution of 2 Å.

    • Main Results:

    • 13 potential ethanol binding sites were identified, with the top three near previously identified bromoethanol sites.
    • Structure refinement yielded a crystallographic agreement factor of 0.097.
    • Ethanol binding did not significantly alter lysozyme's molecular structure or thermal motions.
    • 61% of ethanol-lysozyme contacts were with hydrophobic sites, consistent with ethanol's nature.

    Conclusions:

    • Ethanol interacts predominantly with hydrophobic regions of lysozyme.
    • The observed binding pattern suggests that alcohol-induced denaturation of lysozyme may occur through dehydration at high alcohol concentrations.
    • The study provides atomic-level insights into protein-solvent interactions and denaturation mechanisms.