title: Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?
abstract: The notion that human α-synuclein is an intrinsically disordered monomeric protein was recently challenged by a postulated α-helical tetramer as the physiologically relevant protein structure. The fact that this alleged conformation had evaded detection for so many years was primarily attributed to a widely used denaturation protocol to purify recombinant α-synuclein. In the present paper, we provide in-cell NMR evidence obtained directly in intact Escherichia coli cells that challenges a tetrameric conformation under native in vivo conditions. Although our data cannot rule out the existence of other intracellular protein states, especially in cells of higher organisms, they indicate clearly that inside E. coli α-synuclein is mostly monomeric and disordered.
authors.affiliation: In-cell NMR Group, Department of NMR-Assisted Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Roessle-Strasse 10, Berlin 13125, Germany.
authors.forename: Andres
authors.initials: A
authors.lastname: Binolfi
authors.forename: Francois-Xavier
authors.initials: FX
authors.lastname: Theillet
authors.forename: Philipp
authors.initials: P
authors.lastname: Selenko
mesh_terms: D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D051844:alpha-Synuclein / Q000737:chemistry / Q000378:metabolism*
chemical_list: D051844:alpha-Synuclein