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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: Jun 20, 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

Protein dynamics from single-molecule fluorescence intensity correlation functions.

Irina V Gopich¹, Daniel Nettels, Benjamin Schuler

¹Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. irinag@niddk.nih.gov

The Journal of Chemical Physics

|September 11, 2009

Summary

This summary is machine-generated.

We developed a simple method to analyze fluorescence intensity correlation functions, revealing insights into conformational dynamics during resonance energy transfer. This approach yields an analytic expression for conformational correlation time, aiding in diffusion coefficient determination.

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Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

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Area of Science:

Photophysics and Biophysical Chemistry
Chemical Physics
Spectroscopy

Background:

Fluorescence intensity correlation functions (FICFs) provide insights into molecular dynamics.
Analyzing FICFs in the presence of resonance energy transfer (RET) is crucial for understanding complex molecular systems.
Existing methods may not fully capture conformational dynamics influenced by RET.

Purpose of the Study:

To propose and implement a straightforward procedure for analyzing FICFs in the presence of RET.
To derive an analytic expression for conformational correlation time under specific conditions.
To enable the determination of diffusion coefficients from experimental FICF data.

Main Methods:

Analysis of fluorescence intensity correlation functions.
Modeling conformational dynamics as diffusion in a potential of mean force.
Derivation of an analytic expression for conformational correlation time.
Utilizing photon count rate and equilibrium distribution.

Main Results:

A simple procedure for analyzing FICFs with RET was successfully implemented.
An analytic expression for conformational correlation time was obtained, assuming timescale separation and diffusion-controlled dynamics.
The derived expression allows for the calculation of the diffusion coefficient governing conformational fluctuations.

Conclusions:

The proposed method offers a simplified approach to extract conformational dynamics information from FICFs in RET systems.
The derived analytic expression is valuable for quantifying diffusion coefficients related to conformational changes.
This work contributes to a better understanding of photophysical and conformational dynamics in complex molecular systems.