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Fast protein dynamics probed with infrared vibrational echo experiments.

M D Fayer1

  • 1Department of Chemistry, Stanford University, Stanford, California 94305, USA. fayer@fayerlab.stanford.edu

Annual Review of Physical Chemistry
|April 28, 2001
PubMed
Summary
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Infrared vibrational echo experiments reveal how solvent viscosity affects protein dynamics in myoglobin (Mb). Lower viscosity enhances protein structural fluctuations, impacting the CO ligand

Area of Science:

  • Biophysics
  • Protein Dynamics
  • Spectroscopy

Background:

  • Myoglobin (Mb) is a crucial protein for oxygen transport.
  • Understanding protein dynamics is key to comprehending biological function.
  • Carbon monoxide (CO) binding to myoglobin (Mb-CO) provides a sensitive probe for studying protein dynamics.

Purpose of the Study:

  • To investigate the influence of solvent viscosity and temperature on the dynamics of myoglobin (Mb).
  • To elucidate the coupling mechanism between protein structural fluctuations and the CO ligand at the active site.
  • To explore the role of electric field fluctuations in mediating protein-ligand interactions.

Main Methods:

  • Utilizing Infrared (IR) vibrational echo experiments to measure the dephasing of the CO-stretching mode in Mb-CO.

Related Experiment Videos

  • Conducting temperature and viscosity dependence studies of Mb-CO pure dephasing in various solvents.
  • Analyzing the temperature dependence of pure dephasing in Mb-CO mutations to test dynamic electric field coupling.

    • Main Results:

    • In glassy solvents, Mb-CO dephasing shows a T(1.3) temperature dependence, indicative of glass-like protein dynamics.
    • In liquid solvents, a steeper temperature dependence is observed, influenced by both temperature and decreasing solvent viscosity.
    • Decreasing solvent viscosity correlates with increased protein surface topological fluctuations and internal structural motions.

    Conclusions:

    • Solvent viscosity significantly modulates protein dynamics in myoglobin.
    • Protein structural fluctuations are coupled to the CO ligand via electric field fluctuations from polar residue movements.
    • Mutational analysis supports the dynamic electric field-coupling mechanism as a key factor in protein-ligand interactions.