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An X-ray diffraction analysis of oriented lipid multilayers containing basic proteins.

W MacNaughtan, K A Snook, E Caspi

    Biochimica Et Biophysica Acta
    |August 27, 1985
    PubMed
    Summary
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    X-ray diffraction reveals how basic proteins interact with lipid bilayers. Different proteins, including myelin basic protein, adopt distinct conformations and positions within the membrane structure.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Materials Science

    Background:

    • Understanding protein-lipid interactions is crucial for cell membrane function.
    • Basic proteins play diverse roles in biological systems.
    • Lipid bilayers form the fundamental structure of cell membranes.

    Purpose of the Study:

    • To investigate the structural organization of basic proteins within lipid bilayers.
    • To determine the conformation and distribution of different basic proteins in a model membrane system.
    • To elucidate the molecular interactions between proteins and lipids at the membrane interface.

    Main Methods:

    • Langmuir-Blodgett technique for creating ordered lipid multilayer specimens.
    • X-ray diffraction to record diffraction patterns from protein-lipid multilayers.

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  • Isomorphous exchange using a brominated cholesterol analog to scale electron density profiles.
  • Derivation of electron density profiles across membranes at 6-12 Å resolution.

    • Main Results:

    • Electron density profiles revealed distinct distributions and conformations for polylysine, cytochrome c, and myelin basic protein (MBP) within cerebroside sulphate/cholesterol bilayers.
    • Polylysine adopted a fully extended chain conformation on the bilayer surface.
    • Cytochrome c maintained its native structure, attaching perpendicular to the membrane.
    • MBP associated with lipid headgroups, showing secondary structure and covering significant area in the membrane plane without penetrating the hydrocarbon core.

    Conclusions:

    • Basic proteins exhibit diverse modes of interaction and structural adaptation when incorporated into lipid bilayers.
    • MBP's interaction with lipid headgroups is specific, with limited penetration into the hydrophobic core.
    • The study provides high-resolution structural insights into protein-lipid interactions relevant to membrane biophysics.