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

Antonio Cupane, Grazia Cottone, Matteo Levantino, Giorgio Schirò, Henrik Till Lemke, Diling Zhu, James Michael Glownia, Hyotcherl Ihee, Mathieu Chollet, Marco Cammarata

Risultato della ricerca: Articlepeer review

140 Citazioni (Scopus)


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.
Lingua originaleEnglish
pagine (da-a)1-6
Numero di pagine6
RivistaNature Communications
Stato di pubblicazionePublished - 2015

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.1300.1300???
  • ???subjectarea.asjc.3100.3100???


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