Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser
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.
- Univ. of Palermo (Italy). Dept. of Physics.
- Univ. of Grenoble Alpes and Institute of Structural Biology (France)
- SLAC National Accelerator Laboratory, Menlo Park, CA (Untied States)
- Inst. for Basic Science (IBS), Daejeon (Republic of Korea)
- Republic of Korea
- Univ. of Rennes (France). Dept. of Physics.
- Publication Date:
- OSTI Identifier:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 6; Journal Issue: 3; Journal ID: ISSN 2041-1723
- Nature Publishing Group
- Research Org:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Org:
- USDOE Office of Science (SC)
- Country of Publication:
- United States
- 59 BASIC BIOLOGICAL SCIENCES
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