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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Backbone 1H, 15N, and 13C resonance assignment and secondary structure prediction of HP0495 from Helicobacter pylori
Min-Duk Seo1, Sung Jean Park, Hyun-Jung Kim
1Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Gwanak-gu, Seoul 151-742, Republic of Korea.
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.
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