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Updated: Jun 22, 2026

Dynamic Light-Induced Protein Patterns at Model Membranes

Dynamic Light-Induced Protein Patterns at Model Membranes

Published on: February 23, 2024

Photoreversible conformational changes in membrane proteins using light-responsive surfactants.

Jing Zhang¹, Shao-Chun Wang, C Ted Lee

¹Department of Chemical Engineering and Materials Science, University of Southern California, Los Angeles, 90089-1211, USA.

The Journal of Physical Chemistry. B

|June 3, 2009

Summary

This summary is machine-generated.

Light reversibly controls bacteriorhodopsin protein conformation using a photoresponsive surfactant. Visible light unfolds the protein into micelles, while UV light refolds it within purple membrane bilayers.

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Area of Science:

Biophysics
Structural Biology
Photochemistry

Background:

Bacteriorhodopsin is a key membrane protein.
Controlling protein conformation is crucial for understanding function.
Light-responsive materials offer novel control mechanisms.

Purpose of the Study:

To demonstrate photoreversible control of bacteriorhodopsin conformation.
To investigate the role of a light-responsive surfactant in protein folding.
To establish a novel method for probing membrane protein dynamics.

Main Methods:

Combined UV-vis, FT-IR, and (31)P NMR spectroscopy.
Dynamic Light Scattering (DLS) measurements.
Utilizing an azobenzene-based surfactant for photoisomerization.

Main Results:

Azobenzene surfactant reversibly controlled micellization upon UV/Vis light exposure.
Visible light induced bacteriorhodopsin unfolding into micelles (20s).
UV light induced protein refolding within bilayers (80s).

Conclusions:

Precise, reversible control of protein conformation achieved with light.
Demonstrated a novel technique to probe membrane protein folding and dynamics.
Established a three-stage model for photosurfactant-membrane protein interactions.