title: High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
abstract: We present three novel exclusively heteronuclear 5D (13)C direct-detected NMR experiments, namely (H(N-flip)N)CONCACON, (HCA)CONCACON and (H)CACON(CA)CON, designed for easy sequence-specific resonance assignment of intrinsically disordered proteins (IDPs). The experiments proposed have been optimized to overcome the drawbacks which may dramatically complicate the characterization of IDPs by NMR, namely the small dispersion of chemical shifts and the fast exchange of the amide protons with the solvent. A fast and reliable automatic assignment of α-synuclein chemical shifts was obtained with the Tool for SMFT-based Assignment of Resonances (TSAR) program based on the information provided by these experiments.
authors.affiliation: Bruker BioSpin GmbH, Silberstreifen, 76287, Rheinstetten, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Bermel
authors.forename: Isabella C
authors.initials: IC
authors.lastname: Felli
authors.forename: Leonardo
authors.initials: L
authors.lastname: Gonnelli
authors.forename: Wiktor
authors.initials: W
authors.lastname: Koźmiński
authors.forename: Alessandro
authors.initials: A
authors.lastname: Piai
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
authors.forename: Anna
authors.initials: A
authors.lastname: Zawadzka-Kazimierczuk
mesh_terms: D002247:Carbon Isotopes / Q000737:chemistry; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*
chemical_list: D002247:Carbon Isotopes; D064267:Intrinsically Disordered Proteins