Thermal stability and unfolding pathways of Sso7d and its mutant F31A by molecular dynamics simulation
首发时间:2012-03-09
Abstract:The thermo-stability and unfolding behaviors of a small hyperthermophilic protein Sso7d as well as its single-point mutation F31A are studied by molecular dynamics simulation at temperatures of 300 K and 500 K. Simulations at 300 K show that the F31A mutant displays a much larger flexibility than the wild type, which implies that the mutation obviously decreases the protein’s stability. High temperature simulations at 500 K suggest that the unfolding of these two proteins evolves along different pathways. For the wild-type protein, the C-terminal alpha-helix is melted at the early unfolding stage, whereas it is destroyed much later in the unfolding process of the F31A mutant. Thus, the mutant unfolds faster than its parent protein. Besides, it is found that the triple-stranded antiparallel -sheet in the wild-type protein plays an important role in maintaining the stability of the entire structure.
keywords: hyperthermophilic protein Sso7d single-point mutation molecular dynamics simulation protein unfolding
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用分子动力学模拟研究Sso7d蛋白及其F31A突变体的热稳定性和去折叠路径
摘要:分别用温度为300 K 和 500 K 的分子动力学模拟方法研究了嗜热蛋白Sso7及其单突变体F31A的热稳定性和去折叠性质。300 K的模拟结果显示,突变体比野生型蛋白具有更大的柔性,这意味着突变减少了蛋白质的稳定性。500 K的高温模拟显示,这两种蛋白出现了不同路径的去折叠。对于野生型蛋白,其C端α 螺旋在早期出现去折叠,但对于突变体,该螺旋比较晚才出现去折叠。模拟结果还发现,突变体比野生型蛋白去折叠更快,野生型蛋白的反平行β片在维持整体蛋白的稳定性中起着重要作用。
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用分子动力学模拟研究Sso7d蛋白及其F31A突变体的热稳定性和去折叠路径
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