title: Structural characterisation of a histone domain by projection-decomposition.
abstract: We demonstrate that two projection experiments, a (15)N-HSQC-NOESY-(15)N-HSQC and a (13)C-HSQC-NOESY-(15)N-HSQC, recorded for a histone domain from yeast, contain enough information to support a structural characterisation of the protein. At the temperature used, 298 K, the histone domain exhibits a very high extent of chemical shift degeneracy that is uncharacteristic for a fully folded domain. Nonetheless, a structured core of 67 residues, which is formed by three α-helices and a two-stranded β-sheet is defined by this NOESY data; this core structure was shown earlier to be present at lower temperature. The above two experiments, which together required 18 h of instrument time, are part of a set of five projection experiments acquired during 2.5 days with the goal of complete characterisation of proteins, including full resonance assignment and structure.
authors.affiliation: Biophysics Group, Department of Chemistry, University of Gothenburg, Box 462, 405 30 Gothenburg, Sweden.
authors.forename: Jonas
authors.initials: J
authors.lastname: Fredriksson
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Bermel
authors.forename: Martin
authors.initials: M
authors.lastname: Billeter
mesh_terms: D003198:Computer Simulation; D006657:Histones / Q000737:chemistry* / Q000648:ultrastructure*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D015003:Yeasts / Q000737:chemistry*
chemical_list: D006657:Histones