 |
Journal articles
Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser.
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.
Keywords :
Biological sciences Biochemistry Biophysics
Cited literature [44 references]
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01139805
Contributor : Laurent Jonchère <>
Submitted on : Tuesday, April 7, 2015 - 10:04:31 AM
Last modification on : Tuesday, January 12, 2021 - 4:41:53 PM
Long-term archiving on: : Tuesday, April 18, 2017 - 11:57:46 AM
Contributor : Laurent Jonchère <>
Submitted on : Tuesday, April 7, 2015 - 10:04:31 AM
Last modification on : Tuesday, January 12, 2021 - 4:41:53 PM
Long-term archiving on: : Tuesday, April 18, 2017 - 11:57:46 AM
File
ncomms7772.pdf
Publisher files allowed on an open archive