To be folded or to be unfolded?
To be folded or to be unfolded?
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DOI：
10.1110/ps.04881304
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发表时间：
2004-11-01
期刊：
影响因子：
8
通讯作者：
Galzitskaya, OV
中科院分区：
文献类型：
--
作者：
Garbuzynskiy, SO;Lobanov, MY;Galzitskaya, OV
在“天然未折叠”蛋白质中缺乏有序结构提出了一个普遍的问题：是否存在氨基酸残基的内在特性，这是在生理条件下缺乏固定结构的原因？在这篇文章中，我们证明，一个蛋白质的能力被折叠或被展开可以由氨基酸残基的属性，以形成足够数量的接触在一个球状状态。从单独的氨基酸序列计算的每个残基的预期平均接触数（使用球状蛋白中20个氨基酸残基的平均接触数）可以用作天然未折叠蛋白质的简单指标之一。80个折叠和90个天然未折叠蛋白质的预测准确率达到89%，如果预期的平均接触数作为参数和83%的疏水性的情况下。通过Monte Carlo算法获得的20个氨基酸残基的最佳人工参数集，以最大限度地分离90个天然未折叠和80个折叠蛋白质的集合，表明预测精度的上限为95%。
The lack of ordered structure in "natively unfolded" proteins raises a general question: Are there intrinsic properties of amino acid residues that are responsible for the absence of fixed structure at physiological conditions? In this article, we demonstrate that the competence of a protein to be folded or to be unfolded may be determined by the property of amino acid residues to form a sufficient number of contacts in a globular state. The expected average number of contacts per residue calculated from the amino acid sequence alone (using the average number of contacts for 20 amino acid residues in globular proteins) can be used as one of the simple indicators of natively unfolded proteins. The prediction accuracy for the sets of 80 folded and 90 natively unfolded proteins reaches 89% if the expected average number of contacts is used as a parameter and 83% in the case of hydrophobicity. An optimal set of artificial parameters for 20 amino acid residues obtained by Monte Carlo algorithm to maximally separate the sets of 90 natively unfolded and 80 folded proteins demonstrates the upper limit for prediction accuracy, which is 95%.