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Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser.

Abstract : Light absorption can trigger biologically relevant protein conformational changes. The light-induced structural rearrangement at the level of a photoexcited chromophore is known to occur in the femtosecond timescale and is expected to propagate through the protein as a quake-like intramolecular motion. Here we report direct experimental evidence of such 'proteinquake' observed in myoglobin through femtosecond X-ray solution scattering measurements performed at the Linac Coherent Light Source X-ray free-electron laser. An ultrafast increase of myoglobin radius of gyration occurs within 1 picosecond and is followed by a delayed protein expansion. As the system approaches equilibrium it undergoes damped oscillations with a ~3.6-picosecond time period. Our results unambiguously show how initially localized chemical changes can propagate at the level of the global protein conformation in the picosecond timescale.
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Submitted on : Tuesday, April 7, 2015 - 10:04:31 AM
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Matteo Levantino, Giorgio Schirò, Henrik Till Lemke, Grazia Cottone, James Michael Glownia, et al.. Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser.. Nature Communications, Nature Publishing Group, 2015, 6 (1), pp.6772. ⟨10.1038/ncomms7772⟩. ⟨hal-01139805⟩

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