Huang Ji-Tao, Tian Jing
Department of Biochemistry, Tianjin University of Technology, Tianjin, China.
Proteins. 2006 May 15;63(3):551-4. doi: 10.1002/prot.20911.
The significant correlation between protein folding rates and the sequence-predicted secondary structure suggests that folding rates are largely determined by the amino acid sequence. Here, we present a method for predicting the folding rates of proteins from sequences using the intrinsic properties of amino acids, which does not require any information on secondary structure prediction and structural topology. The contribution of residue to the folding rate is expressed by the residue's Omega value. For a given residue, its Omega depends on the amino acid properties (amino acid rigidity and dislike of amino acid for secondary structures). Our investigation achieves 82% correlation with folding rates determined experimentally for simple, two-state proteins studied until the present, suggesting that the amino acid sequence of a protein is an important determinant of the protein-folding rate and mechanism.
蛋白质折叠速率与序列预测的二级结构之间的显著相关性表明，折叠速率在很大程度上由氨基酸序列决定。在此，我们提出一种利用氨基酸的内在特性从序列预测蛋白质折叠速率的方法，该方法不需要任何关于二级结构预测和结构拓扑的信息。残基对折叠速率的贡献由残基的欧米伽值表示。对于给定的残基，其欧米伽值取决于氨基酸特性（氨基酸刚性和对二级结构的厌恶程度）。我们的研究与目前所研究的简单两态蛋白质的实验测定折叠速率的相关性达到了82%，这表明蛋白质的氨基酸序列是蛋白质折叠速率和机制的一个重要决定因素。
