title: Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins.
abstract: GroEL-protein interactions were characterized by stable isotope-assisted nuclear magnetic resonance (NMR) spectroscopy using chemically denatured bovine rhodanese and an intrinsically disordered protein, α-synuclein, as model ligands. NMR data indicated that proteins tethered to GroEL remain largely unfolded and highly mobile, enabling identification of the interaction hot spots displayed on intrinsically disordered proteins.
authors.affiliation: Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
authors.forename: Noritaka
authors.initials: N
authors.lastname: Nishida
authors.forename: Maho
authors.initials: M
authors.lastname: Yagi-Utsumi
authors.forename: Fumihiro
authors.initials: F
authors.lastname: Motojima
authors.forename: Masasuke
authors.initials: M
authors.lastname: Yoshida
authors.forename: Ichio
authors.initials: I
authors.lastname: Shimada
authors.forename: Koichi
authors.initials: K
authors.lastname: Kato
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry / Q000378:metabolism; D051844:alpha-Synuclein / Q000737:chemistry / Q000378:metabolism
chemical_list: D018834:Chaperonin 60; D064267:Intrinsically Disordered Proteins; D051844:alpha-Synuclein; D013884:Thiosulfate Sulfurtransferase