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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Human ribosomal protein S13: cloning, expression, refolding, and structural stability
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Human ribosomal protein S13: cloning, expression, refolding, and structural stability

机译：人核糖体蛋白S13：克隆，表达，重折叠和结构稳定性

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摘要

The cDNA of human ribosomal protein S13 was cloned into the expression vector pET-15b. Large-scale production of the recombinant protein was carried out in Escherichia coli cells. Protein accumulated in the form of inclusion bodies was isolated, purified, and refolded by dialysis. The recombinant protein was immunologically reactive, interacting with antiserum against native rpS13. The secondary structure content of the refolded protein was analyzed by means of CD spectroscopy. It was found that 43 +/- 5% of amino acids sequence of the protein form alpha-helices and 11 +/- 3% are placed in beta-strands that coincides with theoretical predictions. The beta-strands seem to be located in the extension regions of the rpS13 and do not have homolognous regions in the structure of rpS15 from Thermus thermophilus, which is a prokaryotic homolog of rpS13. The protein structure is stable at a pH range from 4.0 to 8.0 and at low concentrations of urea (up to 3 M). (C) 2004 Elsevier B.V. All rights reserved.
机译：将人核糖体蛋白S13的cDNA克隆到表达载体pET-15b中。重组蛋白的大规模生产是在大肠杆菌细胞中进行的。分离，纯化并以透析形式折叠以包涵体形式积累的蛋白质。重组蛋白具有免疫反应性，与针对天然rpS13的抗血清相互作用。通过CD光谱分析重新折叠的蛋白质的二级结构含量。已经发现，蛋白质的43 +/- 5％的氨基酸序列形成α-螺旋，而11 +/- 3％位于β-链中，这与理论预测相符。 β链似乎位于rpS13的延伸区域，并且在嗜热栖热菌rpS15的rpS15结构中没有同源区域，而嗜热栖热菌是rpS13的原核同源物。蛋白质结构在4.0到8.0的pH范围和低浓度的尿素（最高3 M）下是稳定的。 （C）2004 Elsevier B.V.保留所有权利。

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