幽门螺杆菌HP0495骨架1H, 15N和13C共振分配和二级结构预测。

Min-Duk Seo, Sung Jean Park, Hyun-Jung Kim, Seung-Hyeon Seok, Bong-Jin Lee
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引用次数: 5

摘要

HP0495(瑞士- prot ID;y495_help)是一种来自幽门螺杆菌26695菌株的86个残基假设蛋白。HP0495的功能无法通过序列同源性来鉴定,HP0495属于一个相当独特的序列家族。在这里,我们报道了HP0495序列特异性的骨干共振分配。大约97%的1HN, 15N, 13Calpha, 13Cbeta和13CO共振被明确地分配。我们可以通过分析13Calpha和13Cbeta化学位移与各自随机线圈值的偏差来预测HP0495的二级结构。二级结构预测表明,HP0495由2个α -螺旋和4个β -链组成。本研究为确定HP0495的溶液结构以及研究HP0495与其他幽门螺杆菌蛋白之间的蛋白-蛋白相互作用奠定了基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Backbone 1H, 15N, and 13C resonance assignment and secondary structure prediction of HP0495 from Helicobacter pylori.

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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