菜豆假想蛋白PHA VU_004G136400g的结构与功能预测

Zohaib Bashir, Muhammad Rizwan, Kanwal Mushtaq, Anum Munir, Ishtiaq Ali
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引用次数: 7

摘要

假设蛋白(HPs)是一种蛋白质,它的发生已经被预测,但在体内的功能还没有被制造出来。说明这些HPs的结构和功能的秘密愿景可能同样会促进对不同种类生命中的蛋白质-蛋白质关系或网络的更好理解。菜豆(Phaseolus vulgaris)是世界上最重要的供人类直接食用的食用豆类,也是最重要的供人类食用的谷物豆类,它具有固定大气氮的能力,在可持续农业中具有重要作用。然而,尽管这一作物物种的重要性,其遗传学特征却很少。本研究选择菜豆(Phaseolus vulgaris)假想蛋白进行分析,并利用不同的生物信息学设备和数据库进行建模。一级和二级结构分析表明,XP_007152511.1是一个稳定的疏水蛋白,含有大量α-螺旋;利用SWISS-MODEL服务器进行同源性建模,与XP_007152511.1蛋白的模板同源性较低,证明了该蛋白的新颖性。采用Ab初始策略生成其三维结构。对质量评估和验证参数的一些评估确定生成的蛋白质模型是稳定的,具有真正的高质量。通过ProtFun 2.2和KEGG (KAAS)完成功能分析,推测该蛋白为具有核结构域的翻译因子。该蛋白在翻译过程中具有能量,参与跨膜屏障、信号和细胞过程以及蛋白质结合。进一步的试验批准将有助于预测不同植物和生物中其他尚未鉴定的蛋白质的结构和功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
In Silico Structural and Functional Prediction of Phaseolus vulgaris Hypothetical Protein PHA VU_004G136400g
Hypothetical proteins (HPs) are the proteins whose occurrence has been predicted, yet in vivo function has not been manufactured up. Illustrating the structural and functional confidential visions of these HPs might likewise prompt a superior understanding of the protein-protein relations or networks in diverse varieties of life. Common bean (Phaseolus vulgaris) is the most important food legume for direct human consumption in the world, most important grain legume for human consumption and has a role in sustainable agriculture helping to its ability to fix atmospheric nitrogen. However, in spite of the importance of this crop species, its genetics have been poorly characterized. In the present study, the hypothetical protein of Phaseolus vulgaris (Common bean) was chosen for analysis, and modeling by distinctive Bioinformatics apparatuses and databases. As indicated by primary and secondary structure analysis, XP_007152511.1 is a stable hydrophobic protein containing a noteworthy extent of α-helices; Homology modeling was utilized SWISS-MODEL server where the templates identity with XP_007152511.1 protein was less which demonstrated novelty of our protein. The Ab initial strategy was conducted to produce its 3D structure. A few evaluations of quality assessment and validation parameters determined the generated protein model as stable with genuinely great quality. Functional analysis was completed by ProtFun 2.2, and KEGG (KAAS), recommended that the hypothetical protein is a translation factor with nuclear domain. The protein was observed to be energetic for translation process, involved in trans-membrane barriers, signaling and cellular processes, and protein binding. It is suggested that further test approval would help to anticipate the structures and functions of other uncharacterized proteins of different plants and living being.
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