한국자기공명학회논문지 (Journal of the Korean Magnetic Resonance Society)

한국자기공명학회 (Korean Magnetic Resonance Society)
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Backbone 1H, 15N, and 13C Resonance Assignment and Secondary Structure Prediction of HP1298 from Helicobacter pylori

  • Kim, Won-Je (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lim, Jong-Soo (Advanced Analysis Center, Korea Institute of Science and Technology (KIST)) ;
  • Son, Woo-Sung (Department of Chemistry and Biochemistry University of California) ;
  • Ahn, Hee-Chul (Advanced Analysis Center, Korea Institute of Science and Technology (KIST)) ;
  • Lee, Bong-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • 발행 : 2008.12.20
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초록

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-l based on sequence homology, and HP1298 is included in IF-l family. Here, we report the sequence-specific backbone resonance assignments of HP1298. About 97% of all the $^{1}HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$, and $^{13}CO$ resonances could be assigned unambiguously. We could predict the secondary structure of HP1298, by analyzing the deviation of the $^{13}C{\alpha}$ and $^{13}C{\beta}$ shemical shifts from their respective random coil values. Secondary structure prediction shows that HP1298 consists of six $\beta$-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.

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참고문헌

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