Robert Schneider

Robert Schneider studied biology and physics in Munich (Germany) and Cambridge (USA). During his Ph.D. thesis at the Max Planck Institute for Biophysical Chemistry in Göttingen (Germany), he applied solid-state NMR spectroscopy to membrane and fibrillar proteins.
His work led to a structural model of the inactivated state of a potassium channel as well as of fibrils formed by polyglutamine peptides. After a postdoctoral stay in the same institut, he moved to Grenoble (France) to work on intrinsically disordered proteins and their interactions using solution-state NMR. Since 2014 he holds a position as assistant professor at the University of Lille.
His research interests continue to focus on the study of membrane, fibrillar, and disordered proteins using NMR spectroscopy in solution and in the solid state.

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Nuclear Magnetic Resonance a Compass to Nanoworld (FUN)

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Nuclear Magnetic Resonance a Compass to Nanoworld (FUN)
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Nuclear Magnetic Resonance (NMR) phenomenon is currently exploited for many purposes, including medical imaging using the MRI technique but also the characterization of the structure and the dynamics of matter at atomic scale by NMR spectroscopy, which is a key tool in chemistry, structural biology, pharmacology and material sciences. [...]