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Updated: Jun 24, 2026

Internalization and Observation of Fluorescent Biomolecules in Living Microorganisms via Electroporation

Internalization and Observation of Fluorescent Biomolecules in Living Microorganisms via Electroporation

Published on: February 8, 2015

Fluorescent proteins for single-molecule fluorescence applications.

Britta Seefeldt¹, Robert Kasper, Thorsten Seidel

¹Applied Laser Physics and Laser Spectroscopy, University of Bielefeld, Physics Department, Universitätsstrasse 25, 33615 Bielefeld, Germany.

Journal of Biophotonics

|April 4, 2009

Summary

mCherry fluorescent protein is ideal for single-molecule studies due to its photostability and minimal intensity fluctuations, making it a valuable tool for advanced microscopy techniques.

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Area of Science:

Biophysics
Molecular Biology
Microscopy

Background:

Fluorescent proteins are crucial tools in biological research.
Existing fluorescent proteins have limitations for advanced single-molecule applications.

Purpose of the Study:

To evaluate mCherry, a DsRed derivative, as a fluorophore for single-molecule fluorescence experiments.
To compare mCherry's photophysical properties with other common fluorescent proteins.

Main Methods:

Single-molecule fluorescence spectroscopy.
Ensemble fluorescence measurements.
Photostability and fluorescence intensity fluctuation analysis.

Main Results:

mCherry demonstrated high photostability and rare fluorescence-intensity fluctuations.
Despite lower quantum yield, mCherry's superior photophysics make it suitable for single-molecule applications.
mCherry has a fluorescence lifetime of 1.46 ns.

Conclusions:

mCherry is an excellent alternative for single-molecule fluorescence experiments.
Its spectral characteristics and short lifetime enable accurate tracking, localization, FRET, FLIM, and multicolor applications.