title: Backbone 1H, 15N, and 13C resonance assignment and secondary structure prediction of HP0495 from Helicobacter pylori.
abstract: HP0495 (Swiss-Prot ID; Y495_HELPY) is an 86-residue hypothetical protein from Helicobacter pylori strain 26695. The function of HP0495 cannot be identified based on sequence homology, and HP0495 is included in a fairly unique sequence family. Here, we report the sequence-specific backbone resonance assignments of HP0495. About 97% of all the 1HN, 15N, 13Calpha, 13Cbeta, and 13CO resonances were assigned unambiguously. We could predict the secondary structure of HP0495, by analyzing the deviation of the 13Calpha and 13Cbeta shemical shifts from their respective random coil values. Secondary structure prediction shows that HP0495 consists of two alpha-helices and four beta-strands. This study is a prerequisite for determining the solution structure of HP0495 and investigating the protein-protein interaction between HP0495 and other Helicobacter pylori proteins.
authors.affiliation: Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Gwanak-gu, Seoul 151-742, Republic of Korea.
authors.forename: Min-Duk
authors.initials: MD
authors.lastname: Seo
authors.forename: Sung Jean
authors.initials: SJ
authors.lastname: Park
authors.forename: Hyun-Jung
authors.initials: HJ
authors.lastname: Kim
authors.forename: Seung-Hyeon
authors.initials: SH
authors.lastname: Seok
authors.forename: Bong-Jin
authors.initials: BJ
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D016480:Helicobacter pylori / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D017433:Protein Structure, Secondary; D011522:Protons
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons