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Structural studies of phosvitin in solution and in the solid state.

V Renugopalakrishnan, P M Horowitz, M J Glimcher

    The Journal of Biological Chemistry
    |September 25, 1985
    PubMed
    Summary

    Phosvitin, a key hen egg yolk phosphoprotein, exhibits a dominant beta-sheet secondary structure. This structure is sensitive to environmental factors, with preliminary data suggesting Ca2+ ions decrease beta-sheet content at low pH.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Spectroscopy

    Background:

    • Phosvitin is the primary phosphoprotein in hen egg yolk.
    • Understanding its structure is crucial for comprehending phosphoprotein function.

    Purpose of the Study:

    • To determine the secondary structure of phosvitin in solid and solution states.
    • To propose a structural model for phosvitin.

    Main Methods:

    • Circular dichroism spectroscopy
    • Fourier transform infrared (FTIR) spectroscopy (photoacoustic and fluorescence)
    • Chou-Fasman predictive algorithm

    Main Results:

    • Beta-sheets are the dominant secondary structural component in phosvitin.

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  • A three-compartment model (alpha-helical, beta-sheet, beta-turn) was proposed.
  • Phosvitin's secondary structure is sensitive to environmental factors, including Ca2+ ions.

    • Conclusions:

    • The proposed structural model for phosvitin shares similarities with other phosphoproteins.
    • Environmental factors, particularly Ca2+ ions at low pH, can alter phosvitin's secondary structure.