Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser. - Université de Rennes Access content directly
Journal Articles Nature Communications Year : 2015

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.
Fichier principal
Vignette du fichier
ncomms7772.pdf (714.83 Ko) Télécharger le fichier
Origin Publisher files allowed on an open archive
Loading...

Dates and versions

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

Identifiers

Cite

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⟩
401 View
468 Download

Altmetric

Share

Gmail Mastodon Facebook X LinkedIn More