Skip to Main content Skip to Navigation
Journal articles

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.
Complete list of metadata

Cited literature [44 references]  Display  Hide  Download
Contributor : Laurent Jonchère Connect in order to contact the contributor
Submitted on : Tuesday, April 7, 2015 - 10:04:31 AM
Last modification on : Wednesday, October 20, 2021 - 3:47:03 AM
Long-term archiving on: : Tuesday, April 18, 2017 - 11:57:46 AM


Publisher files allowed on an open archive



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⟩



Record views


Files downloads