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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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Related Experiment Video

Updated: May 18, 2026

A Fluorescence Fluctuation Spectroscopy Assay of Protein-Protein Interactions at Cell-Cell Contacts

A Fluorescence Fluctuation Spectroscopy Assay of Protein-Protein Interactions at Cell-Cell Contacts

Published on: December 1, 2018

Characterizing natural colloidal/particulate-protein interactions using fluorescence-based techniques and principal

Ramila H Peiris¹, Nicholas Ignagni, Hector Budman

¹Department of Chemical Engineering, University of Waterloo, 200 University Avenue West, Waterloo, ON, Canada N2L 3G1.

|September 13, 2012

Summary

This summary is machine-generated.

We developed a rapid and sensitive fluorescence-based method to study interactions between natural particles and proteins. This technique aids understanding of phenomena like membrane fouling and nanoparticle applications.

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Published on: April 6, 2012

Area of Science:

Environmental Science
Biochemistry
Materials Science

Background:

Interactions between natural colloidal/particulate matter and protein-like substances are crucial for understanding membrane fouling, bacterial adhesion, and nanoparticle applications in nanomedicine and nanotoxicology.
Current characterization methods often lack the speed, sensitivity, and accuracy required for precise analysis of these complex interactions.

Purpose of the Study:

To develop and validate a novel fluorescence-based approach for characterizing interactions between natural colloidal/particulate matter and protein-like matter.
To provide a rapid, sensitive, and accurate method for quantifying these interactions at a physical level.

Main Methods:

Utilized fluorescence-based excitation-emission matrix (EEM) spectroscopy combined with principal component analysis (PCA).
Employed surface plasmon resonance (SPR) analysis and fiber-optic probe-based surface fluorescence measurements for validation.

Main Results:

The EEM-PCA approach successfully extracted information regarding colloidal/particulate-protein interactions.
SPR and fiber-optic measurements confirmed the validity of the fluorescence-based method for characterizing these interactions.

Conclusions:

The developed fluorescence-based EEM-PCA method offers a powerful tool for studying colloidal/particulate-protein interactions.
This technique provides a rapid and sensitive alternative for fundamental measurements, with significant implications for environmental science, nanomedicine, and nanotoxicology.