Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser. - Université de Rennes Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2015

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

Résumé

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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Dates et versions

hal-01139805 , version 1 (07-04-2015)

Identifiants

Citer

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, 2015, 6 (1), pp.6772. ⟨10.1038/ncomms7772⟩. ⟨hal-01139805⟩
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