title: Backbone 1H, 15N, and 13C resonance assignment of HP1242 from Helicobacter pylori.
abstract: One of the small proteins from Helicobacter pylori, HP1242, was investigated by the solution nuclear magnetic resonance (NMR) spectroscopy. HP1242 is known as a 76-residue conserved hypothetical protein and its function cannot be identified based on sequence homology. Here, the results of the backbone (1)H, (15)N, and (13)C resonance assignments of the HP1242 are reported using double- and triple-resonance techniques. About 95 % of all of the (1)HN, (15)N, (13)CO, (13)Calpha, and (13)Cbeta resonances that cover 75 non-Proline residues of the 76 residues are clarified through sequential- and specific- assignments. In addition, three helical regions were clearly identified on the basis of the resonance assignments.
authors.affiliation: National Lab. of Membrane Protein Structure (MPS), Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Korea.
authors.forename: Su-Jin
authors.initials: SJ
authors.lastname: Kang
authors.forename: Sung Jean
authors.initials: SJ
authors.lastname: Park
authors.forename: Seo-Jeong
authors.initials: SJ
authors.lastname: Jung
authors.forename: Bong-Jin
authors.initials: BJ
authors.lastname: Lee
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D016480:Helicobacter pylori / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D016366:Open Reading Frames; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins