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Biochemical and Structural Characterization of HP1423 (Y1423_HELPY) from Helicobacter pylori
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  • Biochemical and Structural Characterization of HP1423 (Y1423_HELPY) from Helicobacter pylori
  • Biochemical and Structural Characterization of HP1423 (Y1423_HELPY) from Helicobacter pylori
저자명
Kim. Ji-Hun,Lee. Ki-Young,Park. Sung-Jean,Lee. Bong-Jin
간행물명
Journal of the Korean magnetic resonance society
권/호정보
2010년|14권 1호|pp.45-54 (10 pages)
발행정보
한국자기공명학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

HP1423 (Y1423_HELPY) is a conserved hypothetical protein from H. pylori strain 26695. However, Sequence Blast result indicates that HP1423 belongs to S4 (PF01479) superfamily. According to Pfam database, the S4 domain is a small domain consisting of 60-65 amino acid residues, that probably mediates binding to RNA. In this study, we report the sequence-specific backbone resonance assignment of HP1423, which has 84 amino acid residues. We could assign unambiguously about 88% of all $^{1}H_{N}$, $^{15}N$, $^{13}C_{alpha}$, $^{13}C_{eta}$ and $^{13}C=O$ resonances. We could not detect the resonances from residues 15-20, and disappearance of these peaks seems to be related with the intermediate-conformational exchange. These assigned NMR peaks of HP1423 can be used for studying the role of protein dynamics in millisecond timescale, and Protein-RNA binding.