Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography.

@article{Bourgeois2006ExtendedSS,
  title={Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography.},
  author={D. Bourgeois and B. Vallone and A. Arcovito and G. Sciara and F. Schotte and P. Anfinrud and M. Brunori},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 13},
  pages={
          4924-9
        }
}
Work carried out over the last 30 years unveiled the role of structural dynamics in controlling protein function. Cavity networks modulate structural dynamics trajectories and are functionally relevant; in globins they have been assigned a role in ligand migration and docking. These findings raised renewed interest for time-resolved structural investigations of myoglobin (Mb), a simple heme protein displaying a photosensitive iron-ligand bond. Photodissociation of MbCO generates a… Expand
Dipar Institu Synch Structural Dynamics of Myoglobin
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Time-resolved serial femtosecond crystallography at an x-ray free-electron laser is used to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond and supports the prediction that an immediate collective response of the protein occurs upon ligand dissociation. Expand
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TLDR
This chapter describes some of the technological features involved in obtaining reliable data by time-resolved Laue crystallography, with subnanosecond time resolution. Expand
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Kinetics of carbon monoxide migration and binding in solvated neuroglobin as revealed by molecular dynamics simulations and quantum mechanical calculations.
TLDR
Using multiple (independent) molecular dynamics trajectories (about 500 ns in total), the migration pathways of photolized carbon monoxide within solvated Ngb were analyzed, and a quantitative description of CO migration and corresponding kinetics was obtained. Expand
Tracking ligand-migration pathways of carbonmonoxy myoglobin in crystals at cryogenic temperatures.
TLDR
It is shown that this novel method, extended pulsed-laser pumping of carbonmonoxy myoglobin, promotes ligand migration in the protein matrix by crossing the glass transition temperature repeatedly, and enables the visualization of the migration pathway of the photodissociated ligands in native Mb at cryogenic temperatures. Expand
Myoglobin strikes back
  • M. Brunori
  • Medicine, Chemistry
  • Protein science : a publication of the Protein Society
  • 2010
TLDR
To tackle protein's structural dynamics by innovative biophysical methods, laser flash technology made it possible to obtain molecular movies by time‐resolved Laue crystallography (with ps resolution), and this approach unveiled the complexity of the energy landscape and the structural basis of the stretched interconversion between conformational substates of a protein. Expand
The effects of the L29F mutation on the ligand migration kinetics in crystallized myoglobin as revealed by molecular dynamics simulations
TLDR
MD data indicated a clear correlation between CO location within the protein and the conformation adopted by Phe29, well matching the available experimental data as obtained by time‐resolved X‐ray density maps, and point out the subtle mutual effect between ligand diffusion and protein functional motions possibly explaining the observed dramatic variation of CO exit rate in L29F‐Mb. Expand
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