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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Updated: Sep 28, 2025

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

Using Steady-State Fluorescence Anisotropy to Study Protein Clustering.

Ajeet Chaudhary^1,2, Kay Schneitz³

¹Plant Developmental Biology, TUM School of Life Sciences, Technical University of Munich, Freising, Germany.

Methods in Molecular Biology (Clifton, N.J.)

|March 29, 2022

Summary

Investigating protein interactions in live cells is crucial. This study presents a fluorescence anisotropy method for rapid, reproducible analysis of GFP-tagged protein homotypic interactions with subcellular resolution in live tissue.

Keywords:

Arabidopsis Cell wall Confocal laser scanning microscopy Fluorescence anisotropy Methods Microscopy Plasmodesmata Protein–protein interaction Receptor kinase

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Last Updated: Sep 28, 2025

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

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Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Published on: April 25, 2021

Area of Science:

Cellular biology
Biophysics
Molecular imaging

Background:

Signaling pathways depend on precise protein-protein interactions.
Investigating these interactions in live cells with spatiotemporal control is essential.
Existing methods may lack the required resolution or speed.

Purpose of the Study:

To develop a rapid and reproducible method for studying protein-protein interactions in live cells.
To enable investigation of homotypic interactions with subcellular resolution.
To provide a valuable tool for live tissue imaging.

Main Methods:

Microscope-based fluorescence spectrometry.
Utilizing fluorescence anisotropy.
Employing GFP-labeled fusion proteins.

Main Results:

Demonstrated a rapid and reproducible technique for analyzing homotypic protein interactions.
Achieved spatiotemporal resolution in live cells.
Successfully applied the method to live tissue imaging.

Conclusions:

The described fluorescence anisotropy technique is valuable for studying protein complexes in live cells.
Offers high spatiotemporal and subcellular resolution.
Facilitates the investigation of dynamic protein interactions crucial for signaling pathways.