The relationship between experimentally validated intracellular human protein stability and the features of its solvent accessible surface

The relationship between experimentally validated intracellular human protein stability and the features of its solvent accessible surface
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经实验验证的细胞内人类蛋白质稳定性与其溶剂可及表面特征之间的关系

DOI:
10.1504/ijdmb.2015.066338
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发表时间:
2015-12
影响因子:
0.3
通讯作者:
Han, Ping
Han, Ping
中科院分区:
生物学4区
文献类型:
--
作者:
Song, Xiaofeng;Jing, Yan;Han, Ping

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蛋白质的降解是许多细胞过程的关键,研究降解信号的序列和结构有利于分析蛋白质的稳定性。本文从蛋白质的序列和结构特征出发,深入研究了影响蛋白质降解的内在因素。结果表明,短寿命蛋白质表面的疏水残基比长寿命蛋白质多。短寿命蛋白质的二级结构如卷曲倾向于在表面。短寿命蛋白质表面存在较多的丝氨酸磷酸化位点,短寿命蛋白质比长寿命蛋白质更有可能通过PEST基序的信号启动降解。我们还发现几乎所有的N端残基都暴露在表面上,因此,溶剂可及表面残基的特定特征是影响胞内蛋白质稳定性的关键因素。
Protein degradation is critical for most cellular processes, and investigating the degradation signals in the sequence and structure is beneficial for analysing the protein stability. In this paper, we investigated in depth the intrinsic factors affecting the protein degradation based on the sequence and structure features. The results indicated that there are more hydrophobic residues on the surface of short-lived protein than the long-lived protein. The secondary structure such as coil tends to be on the surface of short-lived protein. There are more serine phosphorylation sites on the short-lived protein surface, and there is higher possibility for the short-lived proteins to start the degradation by signal of PEST motif than long-lived proteins. We also found that almost all of N terminal residues are exposed to be on the surface; therefore, the specific features of the solvent accessible surface residues are the key factors affecting intracellular protein stability.
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