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Computational Analysis of the Hypothetical Protein P9303_05031 from Marine Cyanobacterium

机译:海洋青杆菌假想蛋白P9303_05031的计算分析

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摘要

Prochlorococcus marinus MIT 9303 is a marine cyanobacterium found in sea waters. It was first isolated from a depth of 100 m in the Sargasso Sea in the year 1992. This cyanobacterium serves as a good model system for scientific research due to the presence of many desirable characteristics like smaller in size, ability to perform photosynthesis and the ease of culture maintenance. The genome of this cyanobacterium encodes for about 3022 proteins. Out of these 3022 proteins, few proteins were annotated as hypothetical proteins. We performed a computational study to characterize one of the hypothetical proteins “P9303_05031” to deduce its functional role in the cell using various bioinformatics techniques. After in-depth analysis, this hypothetical protein showed the conserved domain as of Hsp10 of molecular chaperonins of GroES. In this work, we have predicted the bidirectional best hits for the hypothetical protein P9303_05031 followed by the prediction of protein properties such as primary, secondary and tertiary structures. The existence of the Hsp10 domain indicates its role is essential for the folding of proteins during heat shock. This work represents the first structural and physicochemical study of the hypothetical protein P9303_05031 in Prochlorococcus marinus MIT 9303.
机译:Prochlorococcus Marinus Mit 9303是海水中发现的海洋肌氨宫。在1992年,它首先从Sargasso海中的深度分离出来的深度。这种蓝杆菌用作科学研究的良好模型系统,因为存在许多所需的特性,如较小的尺寸更小,能够进行光合作用的能力和容易的能力文化维护。该蓝藻的基因组编码约3022蛋白。在这3022个蛋白中,很少有蛋白质被注释为假想蛋白。我们进行了计算研究,以表征一个假想的蛋白质“P9303_05031”的特征,以使用各种生物信息技术技术在细胞中推导出其功能作用。在深入分析之后,该假想蛋白显示了聚合物的分子伴侣Hsp10的保守域。在这项工作中,我们预测了假设蛋白P9303_05031的双向最佳点击,然后预测蛋白质性质,例如初级,二次和三级结构。 HSP10结构域的存在表明其作用对于在热冲击期间蛋白质的折叠至关重要。这项工作代表了促假假设蛋白P9303_05031在促甲基球菌MIRINUS MIT 9303中的第一个结构和物理化学研究。

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