NMR spectroscopy enables the detection of 15N/13C labelled species in cellular environments, and to monitor in real-time their conformational and chemical modifications. We will outline how this unique ability can be exploited in the fields of in-cell structural biology (1,2,3) and cell signaling by post-translational modifications (PTMs) (4,5,6).

(1) FX Theillet et al. Nature, (2016) Structural disorder of monomeric a-synuclein persists in mammalian cells.
(2) J Danielsson et al. PNAS (2015) Thermodynamics of protein destabilization in live cells.

(3) FX Theillet et al. Chem Rev (2014) Physicochemical properties of cells and their effects on intrinsically disordered proteins.
(4) A Binolfi et al. Nat Commun (2016) Intracellular repair of oxidation-damaged a-synuclein fails to target C-terminal modification sites.
(5) MJ Smith et al. Curr Opin Struct Biol (2015) Real-time NMR monitoring of biological activities in complex physiological environments.
(6) FX Theillet et al. Nat Protoc (2013) Site-specific NMR mapping and time-resolved monitoring of S/T phosphorylation.

François-Xavier Theillet obtained his PhD degree from the Pierre & Marie Curie University, Paris (2009). His project was a partnership between the university and the Pasteur Institut, supervised by Dr. Muriel Delepierre. Later, he was chosen for a postdoctoral fellowship at the Structural Biology Department of the Leibniz Institute for Molecular Pharmacology in Berlin, Germany (2010). Currently, he holds the position of first class researcher of CR1 class in the Biochemistry, Biophysics & Structural Biology Department of the Institute for Integrative Biology of the Cell (I2BC) in Gif-sur-Yvette, France (2015).

He is an expert in NMR techniques and, amongst his last projects, he studied new ways to detect cellular post-translational protein modifications of human p53.