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Related Experiment Videos

A new component in protein fluorescence

J W Longworth

    Annals of the New York Academy of Sciences
    |January 1, 1981
    PubMed
    Summary
    This summary is machine-generated.

    Tryptophan fluorescence is distinct from tyrosine fluorescence, allowing selective excitation. A unique tyrosine fluorescence component in human serum albumin suggests excited-state proton transfer from buried residues.

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    Area of Science:

    • Biochemistry
    • Protein Fluorescence Spectroscopy

    Background:

    • Tryptophyl residues exhibit longer wavelength absorption and fluorescence than tyrosyl residues.
    • Selective excitation of tryptophyl fluorescence is possible due to spectral differences.
    • Tyrosyl fluorescence contributes to protein fluorescence, but its contribution can be challenging to isolate.

    Purpose of the Study:

    • To investigate the spectral properties of tyrosyl residues in native human serum albumin.
    • To identify and characterize an unusual fluorescence component in human serum albumin.
    • To elucidate the mechanism behind the observed spectral differences in tyrosyl fluorescence.

    Main Methods:

    • Selective excitation of protein fluorescence.
    • Spectroscopic analysis of fluorescence emission and excitation spectra.

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  • Comparison of native and denatured protein samples.

    • Main Results:

    • Human serum albumin exhibits a distinct tyrosyl fluorescence component with a maximum at 345 nm.
    • This 345-nm component is attributed to excited singlet state protolysis of buried tyrosyl residues.
    • The component is significantly reduced in denatured serum albumin, suggesting structural dependence.

    Conclusions:

    • The 345-nm fluorescence component arises from an intramolecular proton transfer mechanism involving buried tyrosyl residues.
    • An amino group of a buried lysyl residue is a potential proton acceptor.
    • This finding provides insights into the microenvironment and dynamics of tyrosyl residues in proteins.