title: Selective isotopic unlabeling of proteins using metabolic precursors: application to NMR assignment of intrinsically disordered proteins.
abstract: Selective isotopic unlabeling of proteins can provide important residue-type information as well as reduce congestion of NMR spectra. However, metabolic scrambling often complicates the final isotope-labeling pattern. Here, an array of metabolic precursors is used to perform robust, residue-specific unlabeling of proteins. The resulting isotopic-labeling patterns are predictable and nicely complement NMR experiments that differentiate residue types. This approach has widespread applications, but it is particularly relevant for proteins that lack sequence complexity or a defined tertiary structure.
authors.affiliation: Instituto de Biología Molecular y Celular de Rosario, Suipacha 531, S2002LRK Rosario, Argentina.
authors.forename: Rodolfo M
authors.initials: RM
authors.lastname: Rasia
authors.forename: Bernhard
authors.initials: B
authors.lastname: Brutscher
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Plevin
mesh_terms: D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D018797:Cell Cycle Proteins / Q000737:chemistry*; D007553:Isotope Labeling; D015394:Molecular Structure; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D043244:Ribonuclease III / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D029681:Arabidopsis Proteins; D002247:Carbon Isotopes; D018797:Cell Cycle Proteins; D009587:Nitrogen Isotopes; D025801:Ubiquitin; C402383:DCL1 protein, Arabidopsis; D043244:Ribonuclease III