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Title: 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.
 [1] ;  [2] ;  [3] ;  [1] ;  [3] ;  [3] ;  [3] ;  [4] ;  [5] ;  [1] ;  [6]
  1. Univ. of Palermo (Italy). Dept. of Physics.
  2. Univ. of Grenoble Alpes and Institute of Structural Biology (France)
  3. SLAC National Accelerator Laboratory, Menlo Park, CA (Untied States)
  4. Inst. for Basic Science (IBS), Daejeon (Republic of Korea)
  5. Republic of Korea
  6. 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 Lab., Menlo Park, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC)
Country of Publication:
United States