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

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

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96 Citazioni (Scopus)

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.
Lingua originaleEnglish
Numero di pagine6
RivistaNature Communications
Volume6
Stato di pubblicazionePublished - 2015

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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    Cottone, G., Levantino, M., Cupane, A., Schirò, G., Lemke, H. T., Zhu, D., Glownia, J. M., Ihee, H., Chollet, M., & Cammarata, M. (2015). Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser. Nature Communications, 6.