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Membrane optical activity: some facts and fallacies.

D F Wallach, D A Low, A V Bertland

    Proceedings of the National Academy of Sciences of the United States of America
    |November 1, 1973
    PubMed
    Summary
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    Circular dichroism (CD) spectra of poly(L-lysine) shells computed via Mie theory do not match membrane spectra. Light scattering and turbidity effects explain some discrepancies, but CD is unreliable for membrane protein conformation analysis.

    Area of Science:

    • Biophysics
    • Spectroscopy
    • Polymer Science

    Background:

    • Circular dichroism (CD) is used to study protein conformation.
    • Membrane proteins are challenging to analyze conformationally.
    • Poly(L-lysine) is a model polypeptide with known optical properties.

    Purpose of the Study:

    • To compute and analyze the CD spectra of hypothetical poly(L-lysine) shells.
    • To compare computed CD spectra with experimental membrane spectra.
    • To evaluate the utility of CD spectroscopy for determining membrane protein conformation.

    Main Methods:

    • Mie theory was used to compute CD spectra of spherical poly(L-lysine) shells.
    • Simulations considered various radii, wall thickness, and polypeptide conformations.

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  • Computed spectra were compared to experimental data from diverse biological membranes.

    • Main Results:

    • Significant discrepancies were observed between computed and experimental CD spectra below 215 nm.
    • Light scattering alone does not fully explain the optical activity of membranes with nonhelical content.
    • Turbidity effects may explain anomalies near 233 nm, but not uniquely.

    Conclusions:

    • CD spectroscopy using synthetic polypeptides as standards is unreliable for accurate conformational analysis of soluble and membrane proteins.
    • Current methods for correcting membrane CD spectra may introduce artifacts.
    • Further research is needed to develop reliable methods for membrane protein conformational studies.