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Photoconversion of Purified Fluorescent Proteins and Dual-probe Optical Highlighting in Live Cells

Photoconversion of Purified Fluorescent Proteins and Dual-probe Optical Highlighting in Live Cells

Published on: June 26, 2010

Photoconversion in orange and red fluorescent proteins.

Gert-Jan Kremers¹, Kristin L Hazelwood, Christopher S Murphy

¹Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee, USA.

|April 14, 2009

Summary

Photoconversion is common in orange and red fluorescent proteins. Some red proteins switch to green, and orange proteins convert to far-red, enabling new dual-probe applications.

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Fluorescent proteins are crucial tools in biological research.
Understanding their photophysical properties, like photoconversion, is essential for developing advanced imaging techniques.

Purpose of the Study:

To investigate the prevalence and characteristics of photoconversion in orange and red fluorescent proteins.
To identify fluorescent proteins suitable for dual-probe highlighter applications.

Main Methods:

Screening of 12 orange and red fluorescent proteins.
Characterization of photoconversion events and spectral shifts.

Main Results:

Eight out of 12 tested fluorescent proteins exhibited photoconversion.
Three red fluorescent proteins were switched to a green state.
Two orange variants were photoconverted to a far-red state.
Orange proteins showed the most red-shifted excitation spectra reported to date.

Conclusions:

Photoconversion is a frequent property of orange and red fluorescent proteins.
The identified orange fluorescent proteins are promising for dual-probe highlighter applications due to their unique spectral properties.