title: High-resolution characterization of intrinsic disorder in proteins: expanding the suite of (13)C-detected NMR spectroscopy experiments to determine key observables.
abstract: Order in disorder: The characterization of intrinsically disordered proteins by NMR spectroscopy is a necessity on the one hand and a continuous challenge on the other. We propose two experiments that provide diagnostic parameters to monitor the degree of unfolding of a polypeptide. The test was performed on the yeast Cox17 protein, known to gain its function through maturation from an intrinsically disordered state (see figure).
authors.affiliation: CERM University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy. ivanobertini@cerm.unifi.it
authors.forename: Ivano
authors.initials: I
authors.lastname: Bertini
authors.forename: Isabella C
authors.initials: IC
authors.lastname: Felli
authors.forename: Leonardo
authors.initials: L
authors.lastname: Gonnelli
authors.forename: M V
authors.initials: MV
authors.lastname: Vasantha Kumar
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
mesh_terms: D027682:Cation Transport Proteins / Q000737:chemistry*; D000079922:Copper Transport Proteins; D004220:Disulfides / Q000737:chemistry; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D058767:Protein Unfolding; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
chemical_list: C100359:COX17 protein, S cerevisiae; D027682:Cation Transport Proteins; D000079922:Copper Transport Proteins; D004220:Disulfides; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins