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Functionally relevant protein dynamics monitored by time-resolved quasielastic neutron scattering.

Tatsiana Burankova1, Thomas Hauß2, Jacques Ollivier3

  • 1Institute of Physics, University of Tartu, Tartu, Estonia; Laboratory for Neutron Scattering and Imaging, Paul Scherrer Institute, Villigen PSI, Switzerland.

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Protein dynamics are crucial for function. Light energy drives excess protein fluctuations in bacteriorhodopsin, directly promoting structural changes essential for its proton pump function.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Enzyme Function

Background:

  • Protein conformational flexibility is essential for function, but direct evidence is lacking.
  • Previous studies inferred dynamics-function links indirectly through separate experiments.

Purpose of the Study:

  • To directly investigate the real-time modulation of protein dynamics during the functional cycle.
  • To examine the role of picosecond dynamics in the photocycle of bacteriorhodopsin (BR).

Main Methods:

  • Time-resolved quasielastic neutron scattering (TR-QENS) with in-situ light excitation.
  • Studied native purple membranes of bacteriorhodopsin at controlled hydration levels.
  • Time-resolved absorption difference spectroscopy to monitor photocycle intermediates.

Main Results:

  • Actinic light induced excess protein fluctuations within ~150 μs.
  • These fluctuations decayed with a time constant of 250±50 μs.
  • Decay correlated with the buildup of the M2 intermediate, indicating a role in global structural changes.

Conclusions:

  • Excess protein fluctuations actively promote global structural changes in BR during its photocycle.
  • Challenges the view of dynamics as mere "lubricating grease", suggesting an active role in energy conversion.
  • Highlights the direct involvement of light-modulated protein dynamics in enzyme function.