Imaging molecular interactions in cells by dynamic and static fluorescence 
anisotropy (rFLIM and emFRET)

Lidke, D. S.; Nagy, P.; Barisas, B. G.; Heintzmann, R.; Post, J. N.; Lidke, K. A.; Clayton, A. H. A.; Arndt-Jovin, D. J.; Jovin, T. M.

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Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET)

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Lidke, D. S.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Nagy, P.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Heintzmann, R.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Post, J. N.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Lidke, K. A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Clayton, A. H. A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Arndt-Jovin, D. J.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Jovin, T. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Lidke, D. S., Nagy, P., Barisas, B. G., Heintzmann, R., Post, J. N., Lidke, K. A., et al. (2003). Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET). Biochemical Society Transactions, 31(5), 1020-1027. Retrieved from http://www.biochemsoctrans.org/bst/031/1020/0311020.pdf.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-F1C5-4

Abstract

We report the implementation and exploitation of fluorescence polarization measurements, in the form of anisotropy-lifetime (rFLIM) and resonance energy migration (emFRET) modalities, for wide-field, confocal laser scanning, and flow cytometric microscopy of cells. These methods permit the assessment of rotational motion, association, and proximity of cellular proteins in vivo. They are particularly applicable to probes generated by fusions of Visible Fluorescence Proteins (VFPs), as exemplified by studies of the erbB receptor tyrosine kinases involved in growth-factor mediated signal transduction.