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Related Experiment Videos

Enhanced enzymatic activity through photoreversible conformational changes.

Shao-Chun Wang1, C Ted Lee

  • 1Department of Chemical Engineering and Materials Science, University of Southern California, Los Angeles, California 90089-1211, USA. shaochuw@usc.edu

Biochemistry
|November 23, 2007
PubMed
Summary
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Light-responsive surfactants control lysozyme structure and activity. Visible light unfolds the protein, increasing enzymatic activity, while UV light restores its native state, offering complete photoreversible control.

Area of Science:

  • Biochemistry
  • Materials Science
  • Biophysics

Background:

  • Controlling protein structure and function is crucial for biochemical applications.
  • Photoresponsive surfactants offer a light-inducible method for modulating biomolecular interactions.
  • Lysozyme's structure and enzymatic activity are sensitive to environmental changes.

Purpose of the Study:

  • To investigate the light-induced interaction between a photoresponsive surfactant and lysozyme.
  • To control lysozyme's structure and enzymatic activity using light illumination.
  • To elucidate the mechanism of light-controlled protein unfolding and refolding.

Main Methods:

  • Small-angle neutron scattering (SANS) for structural analysis.
  • Shape-reconstruction analysis of SANS data.

Related Experiment Videos

  • UV-Vis spectroscopy to monitor photoisomerization of the azobenzene surfactant.

    • Main Results:

    • Visible light (trans form) induced lysozyme unfolding and swelling, particularly in the hinge region.
    • UV light (cis form) promoted protein refolding to a near-native state.
    • Enzymatic activity increased 8-fold upon unfolding, with full photoreversibility.

    Conclusions:

    • Photoresponsive surfactants provide precise, light-based control over protein conformation and function.
    • Lysozyme's domain separation and flexibility are modulated by surfactant photoisomerization.
    • This system demonstrates a novel approach for light-controlled enzyme activity and protein engineering.