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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: Oct 2, 2025

Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Bimolecular Fluorescence Complementation to Visualize Protein-Protein Interactions in Cells.

Cassandra R Edgar¹, Jimmy D Dikeakos²

¹Department of Microbiology and Immunology, The University of Western Ontario, London, ON, Canada.

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

|February 26, 2022

Summary

This study introduces a bimolecular fluorescence complementation protocol to visualize intracellular protein-protein interactions. This method aids in understanding diseases and infections by characterizing these vital biological interactions.

Keywords:

Bimolecular fluorescence complementation Microscopy Protein–protein interactions Subcellular localization

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Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Published on: March 9, 2014

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM

Published on: December 22, 2015

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Protein-protein interactions are crucial for understanding cellular functions and are implicated in various human diseases.
Visualizing these interactions in real-time within living cells is essential for biological research.

Purpose of the Study:

To describe a novel protocol for bimolecular fluorescence complementation (BiFC).
To enable direct visualization and characterization of intracellular protein-protein interactions.
To determine the subcellular localization of protein complexes using fluorescence microscopy.

Main Methods:

The study details a bimolecular fluorescence complementation (BiFC) assay.
This technique utilizes split fluorescent proteins to detect protein interactions.
Fluorescence microscopy is employed for visualization and localization.

Main Results:

The developed protocol allows for direct visualization of protein-protein interactions within cells.
The method successfully characterizes the dynamics and localization of interacting proteins.
This technique provides a powerful tool for studying protein complex formation.

Conclusions:

Bimolecular fluorescence complementation offers a robust method for studying protein-protein interactions.
This protocol facilitates the investigation of disease mechanisms at the molecular level.
The technique is valuable for both basic research and understanding disease pathologies.