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Valéry Ozenne

Researcher at University of Bordeaux

Publications -  43
Citations -  1914

Valéry Ozenne is an academic researcher from University of Bordeaux. The author has contributed to research in topics: Intrinsically disordered proteins & Medicine. The author has an hindex of 17, co-authored 31 publications receiving 1626 citations. Previous affiliations of Valéry Ozenne include Centre national de la recherche scientifique & French Institute of Health and Medical Research.

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Flexible-meccano

TL;DR: Flexible-meccano will be useful for researchers who wish to compare experimental data with those expected from a fully disordered protein, researchers who see experimental evidence of deviation from 'random coil' behaviour in their protein, or researchers who are interested in working with a broad ensemble of conformers representing the flexibility of the IDP of interest.
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NMR characterization of long-range order in intrinsically disordered proteins.

TL;DR: This study proposes a combination of paramagnetic relaxation enhancements (PREs) and residual dipolar couplings (RDCs) to define both long-range and local structural features of IDPs in solution, and demonstrates that ASTEROIDS, an ensemble selection algorithm, faithfully reproduces intramolecular contacts, even in the presence of highly diffuse, ill-defined target interactions.
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Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.

TL;DR: This approach allows us to identify local conformational sampling properties of urea-unfolded ubiquitin, which shows that the backbone sampling of certain types of charged or polar amino acids is affected more strongly by urea binding than amino acids with hydrophobic side chains.
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Mapping the Potential Energy Landscape of Intrinsically Disordered Proteins at Amino Acid Resolution

TL;DR: This study identifies combinations of RDCs and CSs that can be used to raise conformational degeneracies inherent to different data types, and applies these approaches to characterize the conformational behavior of two intrinsically disordered proteins, the K18 domain from Tau protein and N(TAIL) from measles virus nucleoprotein.