Backbone 1H, 15N, and 13C Resonance Assignment and Secondary Structure Prediction of HP1298 from Helicobacter pylori

김원재; 임종수; 손우성; 안희철; 이봉진

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자료유형: 학술저널

저자정보: 김원재 임종수 손우성 안희철 이봉진

저널정보: 한국자기공명학회 Journal of the Korean Magnetic Resonance Society Journal of the Korean Magnetic Resonance Society 제12권 제2호

발행연도: 2008.1

수록면: 65 - 73 (9page)

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HP1298 (Swiss-Prot ID ; P65108) is an 72-residue protein from Helicobacter pylori strain 26695. The function of HP1298 was identified as Translation initiation factor IF-1 based on sequence homology, and HP1298 is included in IF-1 family. Here, we report the sequence-specific backbone resonance assignments of HP1298. About 97% of all the 1HN, 15N, 13Cα, 13Cβ, and 13CO resonances could be assigned unambiguously. We could predict the secondary structure of HP1298, by analyzing the deviation of the 13Cα and 13Cβ shemical shifts from their respective random coil values. Secondary structure prediction shows that HP1298 consists of six β-strands. This study is a prerequisite for determining the solution structure of HP1298 and investigating the structure-function relationship of HP1298 . Assigned chemical shift can be used for the study on interaction between HP1298 and other Helicobacter pylori proteins.

#HP1298 #NMR #Backbone assignment #Secondary structure

참고문헌 (20)

참고문헌 신청

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C. Gabriel / 1995 / Protein backbone angle restraints from searching a database for chemical shift and sequence homology / J. Biomol. NMR 13 : 289 ~ 302

D. Forman / 1991 / Association between infection with Helicobacter pylori and risk of gastric cancer: evidence from a prospective investigation / Br. Med. J 302 : 1302 ~ 1305

D. S. Wishart / 1991 / Relationship between nuclear magnetic resonance chemical shift and protein secondary structure / J. Mol. Biol 222 : 311 ~ 333

D. S. Wishart / 1994 / The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data / J. Biomol. NMR 4 :

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