title: Hydrogen exchange of disordered proteins in Escherichia coli.
abstract: A truly disordered protein lacks a stable fold and its backbone amide protons exchange with solvent at rates predicted from studies of unstructured peptides. We have measured the exchange rates of two model disordered proteins, FlgM and α-synuclein, in buffer and in Escherichia coli using the NMR experiment, SOLEXSY. The rates are similar in buffer and cells and are close to the rates predicted from data on small, unstructured peptides. This result indicates that true disorder can persist inside the crowded cellular interior and that weak interactions between proteins and macromolecules in cells do not necessarily affect intrinsic rates of exchange.
authors.affiliation: Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
authors.forename: Austin E
authors.initials: AE
authors.lastname: Smith
authors.forename: Larry Z
authors.initials: LZ
authors.lastname: Zhou
authors.forename: Gary J
authors.initials: GJ
authors.lastname: Pielak
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry*; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry; D051844:alpha-Synuclein / Q000737:chemistry* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D064267:Intrinsically Disordered Proteins; D010455:Peptides; D051844:alpha-Synuclein; C071266:FlgM protein, Bacteria; D006859:Hydrogen
keywords: SOLEXSY; amide proton exchange; in-cell NMR; intrinsically disordered proteins; macromolecular crowding