Olivier WALKER

Doctor
work phone: 0437423545

Research

Structural and dynamical characterization of protein/protein and protein/ligand interactions in the liquid state by means of NMR methods. Methodological developments based on spin relaxation, paramagnetic probes, residual dipolar couplings and Small Angle Neutron Scattering. Free energy calculations based on the combination of metadynamics and NMR to understand interaction processes.

Biography

Olivier Walker is currently Assistant Professor (French Maître de Conférence) in the department of Chemistry and Biochemistry at the University of Lyon (France). He obtained his M.Sc. in physical chemistry in 1997 while he received his Ph.D. degree in physical chemistry from the University of Nancy (France) in 2001 where he developed new NMR methodologies to study the rotational diffusion of small molecules in the liquid state, under the supervision of Pr. Daniel Canet. He joined Pr. David Fushman’s lab in 2002 at the University of Maryland (USA) as a postdoctoral fellow to work on protein/protein interactions and more particularly proteins involved in the Proteasome-Ubiquitin system. He developed different approaches to characterize the structure and dynamics of multi-domain proteins. In 2004, he moved to the Institut des Sciences Analytiques where he focused his research on protein/protein (proteins involved in lysosomal degradation) and protein/ligand interactions (proteins of the Prx family) by nuclear magnetic resonance and computational methods based on GPU technology.

Keywords

NMR, protein, interactions, metadynamics, molecular dynamics, paramagnetism

Publications

Publications HAL de olivier,walker

2016

Journal articles

ref_biblio
Carlos Castaneda, Emma K Dixon, Olivier Walker, Apurva Chaturvedi, Mark A Nakasone, et al.. Linkage via K27 bestows ubiquitin chains with unique properties among polyubiquitins. Structure, Elsevier (Cell Press), 2016, 24 (3), pp.423-436. <10.1016/j.str.2016.01.007>. <hal-01359763>
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2015

Journal articles

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Urszula Nowicka, Daoning Zhang, Olivier Walker, Daria Krutauz, Carlos Castaneda, et al.. DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin. Structure, Elsevier (Cell Press), 2015, 23 (3), pp.542-557. <10.1016/j.str.2015.01.010>. <hal-01187309>
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Laura Troussicot, Florence Guillière, Vittorio Limongelli, Olivier Walker, Jean-Marc Lancelin. Funnel-metadynamics and solution NMR to estimate protein-ligand affinities. Journal of the American Chemical Society, American Chemical Society, 2015, 137 (3), pp.1273-1281. <10.1021/ja511336z>. <hal-01187402>
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2014

Journal articles

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Zoi Erpapazoglou, Olivier Walker, Rosine Haguenauer-Tsapis. Versatile Roles of K63-Linked Ubiquitin Chains in Trafficking. STEM CELLS, AlphaMed Press, 2014, 3 (4), pp.1027-1088. <10.3390/cells3041027>. <hal-01128389>
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2013

Journal articles

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Clémentine Aguirre, Tim Ten Brink, Olivier Walker, Florence Guillière, D. Davesne, et al.. BcL-xL Conformational Changes upon Fragment Binding Revealed by NMR. PLoS ONE, Public Library of Science, 2013, 8, pp.e64400. <10.1371/journal.pone.0064400>. <in2p3-00839023>
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2012

Journal articles

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Anja Lange, Mouhamad-Baligh Ismail, Gwladys Rivière, Maggy Hologne, Denis Lacabanne, et al.. Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR. FEBS Letters, Wiley, 2012, 586 (19), pp.3379-3384. <10.1016/j.febslet.2012.07.047>. <hal-00819142>
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Anja Lange, Carlos Castaneda, Daniela Hoeller, Jean-Marc Lancelin, David Fushman, et al.. Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to lys(63)-linked diubiquitin. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (22), pp.18687-18699. <10.1074/jbc.M111.324954>. <hal-00873866>
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2011

Journal articles

ref_biblio
Anja Lange, Daniela Hoeller, Hans Wienk, Olivier Marcillat, Jean-Marc Lancelin, et al.. NMR Reveals a Different Mode of Binding of the Stam2 VHS Domain to Ubiquitin and Diubiquitin. Biochemistry, American Chemical Society, 2011, 50 (1), pp.48-62. <10.1021/bi101594a>. <hal-00873854>
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