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Related Experiment Video

Updated: Apr 20, 2026

4D Imaging of Protein Aggregation in Live Cells

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Coupled protein diffusion and folding in the cell.

Minghao Guo¹, Hannah Gelman¹, Martin Gruebele²

¹Department of Physics, University of Illinois, Urbana, IL, United States of America.

|December 2, 2014

Summary

This summary is machine-generated.

Protein unfolding in cells slows diffusion, influenced by size and interactions. Researchers tracked protein movement, finding unfolding enzyme phosphoglycerate kinase (PGK) exhibited temperature-dependent diffusion changes, possibly due to chaperone binding.

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4D Imaging of Protein Aggregation in Live Cells

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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Area of Science:

Cellular biology
Biophysics
Protein dynamics

Background:

Protein unfolding in cells increases hydrodynamic radius and exposes hydrophobic residues, affecting diffusion.
Cytoplasmic components, including chaperones, can interact with unfolded proteins, further altering their movement.

Purpose of the Study:

To characterize protein diffusion within living cells using advanced imaging techniques.
To investigate the temperature-dependent diffusion of a destabilized enzyme mutant (phosphoglycerate kinase, PGK) and compare it to a stable control.

Main Methods:

Single-point photobleaching of fluorescently labeled proteins in whole cells.
Imaging concentration changes over time to analyze diffusion dynamics.
Applying 2-D or 3-D diffusion equations coupled with a clustering algorithm to model anomalous diffusion.

Main Results:

Green fluorescent protein (GFP) diffusion was characterized as a reference.
Destabilized PGK showed non-monotonic temperature-dependent diffusion, indicating "sticking" during unfolding.
The observed diffusion changes for PGK exceeded predictions from simple size-scaling models.

Conclusions:

Protein unfolding significantly impacts intracellular diffusion, with effects beyond simple hydrodynamic radius changes.
Chaperone binding is a plausible explanation for the observed slower diffusion of unfolding PGK, though other factors may contribute.