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Nat Commun. 2015 Apr 2;6:6772. doi: 10.1038/ncomms7772.

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

Author information

1
Department of Physics and Chemistry, University of Palermo, Palermo 90128, Italy.
2
CNRS, Université Grenoble Alpes, CEA-Institut de Biologie Structurale, Grenoble 38044, France.
3
LCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
4
1] Center for Nanomaterials and Chemical Reactions, Institute for Basic Science (IBS), Daejeon 305-701, Republic of Korea [2] Department of Chemistry, KAIST, Daejeon 305-701, Republic of Korea.
5
Department of Physics, UMR UR1-CNRS 6251, University of Rennes 1, Rennes 35042, France.

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.

PMID:
25832715
PMCID:
PMC4396393
DOI:
10.1038/ncomms7772
[Indexed for MEDLINE]
Free PMC Article

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