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On spectral relaxation in proteins.

¹University of Maryland School of Medicine, Center for Fluorescence Spectroscopy, Department of Biochemistry and Molecular Biology, Baltimore, USA.

Photochemistry and Photobiology

|October 25, 2000

Summary

Time-dependent spectral relaxation is a key factor in the nonexponential fluorescence decay of proteins, particularly single tryptophan proteins (STP). This phenomenon, occurring on a subnanosecond timescale, influences fluorescence interpretations.

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Area of Science:

Biophysics
Protein Fluorescence Spectroscopy

Background:

Debate exists regarding the origins of nonexponential intensity decays in intrinsic tryptophan (trp) fluorescence of proteins.
Single tryptophan proteins (STP) are of particular interest in these studies.

Purpose of the Study:

To review evidence for time-dependent spectral relaxation as a ubiquitous feature of protein fluorescence.
To highlight the significance of spectral relaxation in interpreting fluorescence decay data.

Main Methods:

Analysis of data from diverse sources on protein fluorescence decay.
Examination of observations including wavelength-dependent decay times, decay-associated spectra, and effects of collisional quenching.
Review of time-resolved emission spectra.

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Main Results:

Protein fluorescence decay times increase with observation wavelength.
Longer wavelength components exhibit longer decay times in decay-associated spectra.
Collisional quenching typically shifts emission spectra to shorter wavelengths.
Time-resolved emission spectra show time-dependent shifts to longer wavelengths, consistent with subnanosecond spectral relaxation.

Conclusions:

Time-dependent spectral relaxation is a ubiquitous feature of protein fluorescence, occurring on a subnanosecond timescale.
Spectral relaxation is a significant, potentially dominant, source of nonexponential decay in single tryptophan proteins.
This phenomenon must be considered when interpreting intrinsic protein fluorescence decay.