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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: Aug 26, 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

Extending fluorescence anisotropy to large complexes using reversibly switchable proteins.

Andrea Volpato¹, Dirk Ollech¹, Jonatan Alvelid¹

¹Department of Applied Physics and Science for Life Laboratory, KTH Royal Institute of Technology, Stockholm, Sweden.

Nature Biotechnology

|October 10, 2022

Summary

This summary is machine-generated.

We developed Selective Time-Resolved Anisotropy with Reversibly Switchable States (STARSS) to measure large molecular complexes. This new method extends the observable mass range, enabling study of the entire human proteome.

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Last Updated: Aug 26, 2025

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

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Published on: March 14, 2019

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

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

Published on: April 25, 2025

Area of Science:

Biophysics
Molecular Biology
Cell Biology

Background:

Time-resolved fluorescence anisotropy measures macromolecular complex formation by detecting changes in rotational mobility.
This technique is limited to small molecules (0.1-30 kDa), excluding most of the human proteome.

Purpose of the Study:

To overcome the mass limitation of existing methods for studying macromolecular complexes.
To introduce a novel technique applicable to the entire human proteome.

Main Methods:

Developed Selective Time-Resolved Anisotropy with Reversibly Switchable States (STARSS).
STARSS utilizes long-lived reversible molecular transitions of switchable fluorescent proteins.
This allows resolution of the slow rotational diffusivity characteristic of large complexes.

Main Results:

Extended the observable mass range for rotational mobility measurements by over three orders of magnitude.
Successfully probed the rotational mobility of large cellular complexes, including chromatin, retroviral Gag lattices, and activity-regulated cytoskeleton-associated protein oligomers.
Demonstrated the general applicability of STARSS to arbitrarily large structures.

Conclusions:

STARSS significantly expands the capability to study macromolecular complex formation in cells.
This method is broadly applicable to the vast majority of the human proteome, including large complexes previously inaccessible.
STARSS provides a powerful new tool for molecular and cell biology research.