Thermodynamic analysis of protein sequence-structure relationships in monomer and dimer forms
Thermodynamic analysis of protein sequence-structure relationships in monomer and dimer forms
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DOI：
10.1016/j.physa.2005.03.006
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发表时间：
2005-08
影响因子：
3.3
通讯作者：
Z. R. Li;Gui-rong Liu;Yuan Cheng
中科院分区：
文献类型：
--
作者：
Z. R. Li;Gui-rong Liu;Yuan Cheng
采用二维格点模型分析了HP和YhHX蛋白质序列之间的序列-结构关系以及单体和同源二聚体形式的紧密结构。我们的研究结果表明，大多数结构编码的正常和朊病毒蛋白质序列，和大约三分之一的蛋白质序列是潜在的能够重新折叠从其天然单体构象的替代后二聚体。这些结果部分反映了生物体内蛋白质二聚体和寡聚体结构的存在以及单体蛋白质病理性二聚化或聚集的发生。据观察，蛋白质序列在菌株的数量上有很大差异。从统计学上讲，蛋白质序列的数量随着菌株的数量呈指数下降。使用各种能量参数的计算表明，16个残基序列的最大应变数的期望值大约是它的长度。
Two-dimensional lattice model is employed to analyze the sequence–structure relationships between HP and YhHX protein sequences and compact structures in monomer and homodimer forms. Our results show that most structures are encoded by normal and prion protein sequences, and about one-third of the protein sequences are potentially able to refold from its native monomer conformation to alternative ones upon dimerization thermodynamically. Such findings partially reflect the existences of the dimer and oligomer protein structures in living organism and the occurrence of pathologic dimerization or aggregation of monomer proteins. It is observed that protein sequences differ drastically in the number of strains. Statistically, the number of protein sequences decreases exponentially with the number of strains. Calculations using various energy parameters show that the expected value of maximum number of strains for a 16-residue sequence is about its length.