祝友朋, 韩长志. 粘绿木霉Gv29-8碳水化合物酶类蛋白理化性质预测分析[J]. 西南林业大学学报(自然科学), 2020, 40(4): 74–79 . DOI: 10.11929/j.swfu.201905001
引用本文: 祝友朋, 韩长志. 粘绿木霉Gv29-8碳水化合物酶类蛋白理化性质预测分析[J]. 西南林业大学学报(自然科学), 2020, 40(4): 74–79 . DOI: 10.11929/j.swfu.201905001
Youpeng Zhu, Changzhi Han. Prediction and Analysis of Physicochemical Properties for CAZymes Protein from Trichoderma virens Gv29-8 Genome[J]. Journal of Southwest Forestry University, 2020, 40(4): 74-79. DOI: 10.11929/j.swfu.201905001
Citation: Youpeng Zhu, Changzhi Han. Prediction and Analysis of Physicochemical Properties for CAZymes Protein from Trichoderma virens Gv29-8 Genome[J]. Journal of Southwest Forestry University, 2020, 40(4): 74-79. DOI: 10.11929/j.swfu.201905001

粘绿木霉Gv29-8碳水化合物酶类蛋白理化性质预测分析

Prediction and Analysis of Physicochemical Properties for CAZymes Protein from Trichoderma virens Gv29-8 Genome

  • 摘要: 粘绿木霉Gv29-8是已完成全基因组测序的重要生防拮抗菌之一,为对其碳水化合物酶类蛋白的理化性质进行预测分析,以粘绿木霉中185个CAZymes蛋白序列为研究对象,对其理化性质进行了预测分析。结果表明:近2/3的蛋白理论等电点(pI)小于6,属于酸性蛋白,同时,通过随机数软件对上述蛋白进行10%随机抽样分析,发现不同理论等电点类别的CAZymes蛋白所具有的分子式、原子数量、半衰期、不稳定性系数、脂肪族氨基酸指数、总平均亲水性等性质不尽相同。其中,比例为26.67%的蛋白属于不稳定蛋白,比例为13.33%的蛋白属于亲水性蛋白。

     

    Abstract: Trichoderma virens Gv29-8 is one of the important biocontrol antagonists that have completed genome-wide sequencing. In order to predict and analyze the physicochemical properties of carbohydrate-active enzymes protein (CAZymes), 185 CAZymes proteins sequence in the T. virens Gv29-8 obtained in the previous period were the objects of the research, and the physicochemical properties were predicted and analyzed. The results showed that nearly two-thirds proteins theoretical isoelectric points (PI) is less than 6, which are acidic protein. At the same time, 10% random sampling analysis of the above proteins by the random number software, and it was found that the CAZymes proteins of different theoretical isoelectric points categories have different physicochemical properties such as molecular formula, atomic number, half-life, instability coefficient, aliphatic amino acid index and total average hydrophilicity. Among them, 26.67% of the proteins belong to unstable proteins and 13.33% of the proteins belong to hydrophilic proteins.

     

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