V
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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Journal ArticleDOI
Flexible-meccano
Valéry Ozenne,Frédéric Bauer,Loïc Salmon,Jie Rong Huang,Malene Ringkjøbing Jensen,Stéphane Segard,Pau Bernadó,Céline Charavay,Martin Blackledge +8 more
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.
Journal ArticleDOI
NMR characterization of long-range order in intrinsically disordered proteins.
Loïc Salmon,Gabrielle Nodet,Valéry Ozenne,Guowei Yin,Malene Ringkjøbing Jensen,Markus Zweckstetter,Martin Blackledge +6 more
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.
Journal ArticleDOI
Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.
Gabrielle Nodet,Loïc Salmon,Valéry Ozenne,Sebastian Meier,Malene Ringkjøbing Jensen,Martin Blackledge +5 more
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.
Journal ArticleDOI
Predictive atomic resolution descriptions of intrinsically disordered hTau40 and α-synuclein in solution from NMR and small angle scattering.
Martin Schwalbe,Valéry Ozenne,Valéry Ozenne,Stefan Bibow,Mariusz Jaremko,Lukasz Jaremko,Michal J. Gajda,Malene Ringkjøbing Jensen,Malene Ringkjøbing Jensen,Jacek Biernat,Stefan Becker,Eckhard Mandelkow,Markus Zweckstetter,Martin Blackledge,Martin Blackledge +14 more
TL;DR: Extensive cross-validation is shown that five different types of independent experimental parameters are predicted more accurately by selected ensembles than by statistical coil descriptions, suggesting that this region of conformational space is important for aggregation.
Journal ArticleDOI
Mapping the Potential Energy Landscape of Intrinsically Disordered Proteins at Amino Acid Resolution
Valéry Ozenne,Robert Schneider,Mingxi Yao,Jie Rong Huang,Loïc Salmon,Markus Zweckstetter,Malene Ringkjøbing Jensen,Martin Blackledge +7 more
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.