Nature of driving force for protein folding: A result from analyzing the statistical potential
Nature of driving force for protein folding: A result from analyzing the statistical potential
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DOI：
10.1103/physrevlett.79.765
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发表时间：
1997-07-28
影响因子：
8.6
通讯作者：
Wingreen, NS
中科院分区：
文献类型：
--
作者：
Li, H;Tang, C;Wingreen, NS
在蛋白质结构分析的统计方法中，Miyazawa和Jernigan导出了不同类型氨基酸之间残基间接触能的20 X 20矩阵。利用特征值分解的方法，我们发现Miyazawa-Jernigan矩阵可以由其前两个主成分向量精确地重建为M-ij = C-0 + C-1（q（i））+ q（i））+ C（2）q（i）q（i），其中C为常数，q值与20个氨基酸相关。这种规律性是由于疏水相互作用和分层力，后者服从简单液体的希尔德布兰德溶解度理论。
In a statistical approach to protein structure analysis, Miyazawa and Jernigan derived a 20 X 20 matrix of inter-residue contact energies between different types of amino acids. Using the method of eigenvalue decomposition, we find that the Miyazawa-Jernigan matrix can be accurately reconstructed from its first two principal component vectors as M-ij = C-0 + C-1(q(i)) + q(i)) + C(2)q(i)q(i), with constant C's, and 20 q values associated with the 20 amino acids. This regularity is due to hydrophobic interactions and a force of demixing, the latter obeying Hildebrand's solubility theory of simple liquids.