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Dominique Bourgeois

Researcher at University of Grenoble

Publications -  119
Citations -  6042

Dominique Bourgeois is an academic researcher from University of Grenoble. The author has contributed to research in topics: Chromophore & Fluorescence. The author has an hindex of 41, co-authored 110 publications receiving 5559 citations. Previous affiliations of Dominique Bourgeois include European Synchrotron Radiation Facility & Centre national de la recherche scientifique.

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Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography.

TL;DR: Time-resolving experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results and molecular dynamics calculations, and demonstrate that time-resolved macromolecular crystallography can elucidate the structural bases of biochemical mechanisms on the nanosecond time scale.
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Protein Conformational Relaxation and Ligand Migration in Myoglobin: A Nanosecond to Millisecond Molecular Movie from Time-Resolved Laue X-ray Diffraction†

TL;DR: These results demonstrate that structural changes as small as 0.2 A and populations of CO docking sites of 10% can be detected by time-resolved X-ray diffraction.
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Energy transduction on the nanosecond time scale: early structural events in a xanthopsin photocycle.

TL;DR: Direct structural evidence is provided for the initial processes of transduction of light energy, which ultimately translate into a physiological signal.
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Structural characterization of IrisFP, an optical highlighter undergoing multiple photo-induced transformations

TL;DR: In this article, the Phe-173-Ser mutant of the tetrameric variant of EosFP, named IrisFP, was characterized using both crystallography and (in crystallo) spectroscopy.
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Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography.

TL;DR: It is proposed that the extended relaxation of the globin moiety reflects reequilibration among conformational substates known to play an essential role in controlling protein function.