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Electron diffraction study of the hexagonal polymorphic form of some choline-containing phosphpolipids.

D L Dorset

    Biochimica Et Biophysica Acta
    |February 20, 1975
    PubMed
    Summary
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    Electron diffraction reveals helical twisting in phospholipid aliphatic chains, suggesting a novel packing model for these organic crystals. This study proposes translational disorders along the chain axes in lecithin crystals.

    Area of Science:

    • Structural biology
    • Crystallography
    • Biophysics

    Background:

    • The kinematical diffraction assumption is suitable for analyzing electron diffraction patterns from thin organic crystals.
    • Phospholipids, such as lecithin, lysolecithin, and sphingomyelin, are crucial biological molecules with complex aliphatic chain structures.

    Purpose of the Study:

    • To analyze the crystal structure of anhydrous microcrystals of lecithin, lysolecithin, and beef brain sphingomyelin using electron diffraction.
    • To investigate the packing model of aliphatic chains within these phospholipid molecules.
    • To explore potential disorders in the aliphatic chain arrangement.

    Main Methods:

    • Obtaining single crystal electron diffraction patterns from thin anhydrous microcrystals.
    • Performing crystal structure analysis using hk0 intensity data.

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  • Applying the kinematical diffraction assumption for pattern analysis.

    • Main Results:

    • The hk0 intensity data confirmed a free methylene rotor model for the projection of aliphatic chain packing.
    • Evidence suggests helical twisting along the polymethylene chains, differing from rigid body rotation in paraffins.
    • Lecithin crystals lacked upper layer diffraction, indicating translational disorders along the chain axes.

    Conclusions:

    • The study validates a specific packing model for aliphatic chains in phospholipids.
    • Helical twisting is proposed as the mechanism for aliphatic chain arrangement in phospholipids.
    • Translational disorders are suggested along the chain axes in lecithin crystals, impacting their structural properties.