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Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser
Matteo Levantino1, Giorgio Schirò2, Henrik Till Lemke3
1Department of Physics and Chemistry, University of Palermo, Palermo 90128, Italy.
Nature Communications
|April 3, 2015
Summary
Protein structural changes, termed
Area of Science:
- Structural Biology
- Biophysics
- Photochemistry
Background:
- Light absorption induces protein conformational changes.
- Photoexcited chromophores initiate ultrafast structural rearrangements.
- These changes are hypothesized to propagate as intramolecular motions.
Purpose of the Study:
- To provide direct experimental evidence of light-induced protein conformational changes.
- To investigate the propagation dynamics of photoexcited chromophore events in proteins.
- To observe the 'proteinquake' phenomenon in myoglobin.
Main Methods:
- Femtosecond X-ray solution scattering (fs-XSS) measurements.
- Utilized the Linac Coherent Light Source (LCLS) X-ray free-electron laser.
- Studied the dynamics of myoglobin following photoexcitation.
Main Results:
- Observed an ultrafast increase in myoglobin's radius of gyration within 1 picosecond.
- Detected a subsequent delayed protein expansion.
- Observed damped oscillations with a ~3.6-picosecond period as the system approached equilibrium.
Conclusions:
- Directly observed 'proteinquake' phenomenon in myoglobin.
- Demonstrated propagation of localized chemical changes to global protein conformation on picosecond timescales.
- Provided experimental validation for light-induced intramolecular motions in proteins.
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