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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 9, 2025

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Published on: August 27, 2014

An Ultrastable and Dense Single-Molecule Click Platform for Sensing Protein-Deoxyribonucleic Acid Interactions.

Emiel W A Visser^1,2, Jovana Miladinovic¹, Joshua N Milstein^1,3

¹Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, ON L5L 1C6, Canada.

|December 20, 2021

Summary

A new single-molecule assay uses advanced click chemistry for ultra-stable protein-DNA interaction studies. This method enhances density and stability, enabling new research into bacterial protein binding dynamics.

Keywords:

biomarker sensing platforms click-chemistry high-stability histone-like nucleoid-structuring proteins protein-deoxyribonucleic acid interactions tethered particle motion

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Protein-DNA interactions are crucial for cellular processes.
Existing single-molecule assays have limitations in stability and density.
Understanding these interactions requires advanced observational techniques.

Purpose of the Study:

To develop an ultrastable, highly dense single-molecule assay for observing protein-DNA interactions.
To improve upon existing tethered particle motion assays.
To enable the study of previously inaccessible sequence and temperature-dependent effects.

Main Methods:

Utilized next-generation click chemistry for stable tethering of reporter particles.
Achieved ultrahigh density of surface-tethered particles.
Tested assay stability at elevated temperatures (up to 45°C) and compatibility with Mg²⁺.

Main Results:

Demonstrated an ultrastable and highly dense single-molecule assay.
The assay showed low non-specific interactions and stability for over 6 months.
Enabled study of sequence and temperature effects on bacterial histone-like nucleoid-structuring protein binding to DNA.

Conclusions:

The developed assay significantly advances the study of protein-DNA interactions.
It offers improved stability, density, and compatibility for biomolecular studies.
The assay is readily translatable to enhance single-molecule biosensing applications.