title: Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.
abstract: We present an integrated approach for efficient characterization of intrinsically disordered proteins. Batch cell-free expression, fast data acquisition, automated analysis, and statistical validation with data resampling have been combined for achieving cost-effective protein expression, and rapid automated backbone assignment. The new methodology is applied for characterization of five cytosolic domains from T- and B-cell receptors in solution.
authors.affiliation: Swedish NMR Centre, University of Gothenburg, Gothenburg, Sweden.
authors.forename: Linnéa
authors.initials: L
authors.lastname: Isaksson
authors.forename: Maxim
authors.initials: M
authors.lastname: Mayzel
authors.forename: Maria
authors.initials: M
authors.lastname: Saline
authors.forename: Anders
authors.initials: A
authors.lastname: Pedersen
authors.forename: Joakim
authors.initials: J
authors.lastname: Rosenlöw
authors.forename: Bernhard
authors.initials: B
authors.lastname: Brutscher
authors.forename: B Göran
authors.initials: BG
authors.lastname: Karlsson
authors.forename: Vladislav Y
authors.initials: VY
authors.lastname: Orekhov
mesh_terms: D020816:Amino Acid Motifs; D003600:Cytosol / Q000378:metabolism; D006801:Humans; D042541:Intracellular Space / Q000378:metabolism; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017434:Protein Structure, Tertiary; D011947:Receptors, Antigen, B-Cell / Q000737:chemistry* / Q000378:metabolism; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D064267:Intrinsically Disordered Proteins; D008024:Ligands; D011947:Receptors, Antigen, B-Cell; D011948:Receptors, Antigen, T-Cell