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

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Title
Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser
Author(s)
Levantino M.; Schiro G.; Lemke H.T.; Cottone G.; Glownia J.M.; Zhu D.; Chollet M.; Hyotcherl Ihee; Cupane A.; Cammarata M.
Publication Date
2015-04
Journal
NATURE COMMUNICATIONS, v.6, no., pp.6772 -
Publisher
NATURE PUBLISHING GROUP
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. © 2015 Macmillan Publishers Limited. All rights reserved
URI
http://pr.ibs.re.kr/handle/8788114/1626
DOI
10.1038/ncomms7772
ISSN
2041-1723
Appears in Collections:
Center for Nanomaterials and Chemical Reactions(나노물질 및 화학반응 연구단) > Journal Papers (저널논문)
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