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Updated: Aug 29, 2026

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
Published on: December 11, 2021
Picosecond time-resolved microspectrofluorometry in live cells exemplified by complex fluorescence dynamics of
M Tramier1, K Kemnitz, C Durieux
1Institut Jacques Monod, UMR 7592, CNRS, Universités P6/P7, 75251 Paris Cedex 05, France. tramier@ijm.jussieu.fr
Abstract:
Time-resolved microspectrofluorometry in live cells, based on time- and space-correlated single-photon counting, is a novel method to acquire spectrally resolved fluorescence decays, simultaneously in 256 wavelength channels. The system is calibrated with a full width at half maximum (FWHM) of 90 ps for the temporal resolution, a signal-to-noise ratio of 10(6), and a spectral resolution of 30 (Deltalambda/Lambda). As an example, complex fluorescence dynamics of ethidium and cyan fluorescent protein (CFP) in live cells are presented. Free and DNA intercalated forms of ethidium are simultaneously distinguishable by their relative lifetime (1.7 ns and 21.6 ns) and intensity spectra (shift of 7 nm). By analysing the complicated spectrally resolved fluorescence decay of CFP, we propose a fluorescence kinetics model for its excitation/desexcitation process. Such detailed studies under the microscope and in live cells are very promising for fluorescence signal quantification.
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