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E-type delayed fluorescence depolarization, technique to probe rotational motion in the microsecond range

R Greinert, H Staerk, A Stier

    Journal of Biochemical and Biophysical Methods
    |May 1, 1979
    PubMed
    Summary
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    Eosin-type delayed fluorescence depolarization studies enable the measurement of slow molecular rotational diffusion, particularly for membrane proteins. This technique allows investigation of macromolecular movement over microsecond to millisecond timescales.

    Area of Science:

    • Biophysics
    • Biochemistry
    • Membrane Protein Dynamics

    Background:

    • Investigating slow rotational movement of macromolecules like membrane proteins requires techniques with extended time ranges.
    • Existing methods may not adequately cover the microsecond to millisecond timescale for rotational diffusion.

    Purpose of the Study:

    • To extend the time range for measuring rotational diffusion to microseconds and milliseconds.
    • To enable the investigation of slow rotational movement of macromolecules, such as membrane proteins.
    • To describe an apparatus for determining time-dependent anisotropy in this time range.

    Main Methods:

    • Utilizing eosin (E)-type delayed fluorescence depolarization.
    • Measuring time-dependent anisotropy.

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  • Employing an apparatus designed for microsecond to millisecond timescales.

    • Main Results:

    • Eosin-type delayed fluorescence depolarization successfully extends the measurement time range for rotational diffusion.
    • The method allows for the investigation of slow rotational movement of macromolecules.
    • The described apparatus is suitable for determining time-dependent anisotropy in the microsecond to millisecond range.

    Conclusions:

    • Eosin-type delayed fluorescence depolarization is a valuable technique for studying slow macromolecular rotational dynamics.
    • The developed apparatus effectively measures time-dependent anisotropy in the microsecond to millisecond range.
    • The method was validated using eosin-labelled cytochrome P-450 in phospholipid membrane vesicles.