State Key Laboratory of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin 300071, China.
Amino Acids. 2012 Aug;43(2):567-72. doi: 10.1007/s00726-011-1189-3. Epub 2011 Dec 13.
The successful prediction of protein-folding rates based on the sequence-predicted secondary structure suggests that the folding rates might be predicted from sequence alone. To pursue this question, we directly predict the folding rates from amino acid sequences, which do not require any information on secondary or tertiary structure. Our work achieves 88% correlation with folding rates determined experimentally for proteins of all folding types and peptide, suggesting that almost all of the information needed to specify a protein's folding kinetics and mechanism is comprised within its amino acid sequence. The influence of residue on folding rate is related to amino acid properties. Hydrophobic character of amino acids may be an important determinant of folding kinetics, whereas other properties, size, flexibility, polarity and isoelectric point, of amino acids have contributed little to the folding rate constant.
基于序列预测二级结构成功预测蛋白质折叠速率表明，折叠速率可能仅通过序列预测。为了探究这个问题，我们直接从氨基酸序列预测折叠速率，这不需要任何有关二级或三级结构的信息。我们的工作实现了与所有折叠类型的蛋白质和肽的实验确定折叠速率的 88%的相关性，表明指定蛋白质折叠动力学和机制所需的几乎所有信息都包含在其氨基酸序列中。残基对折叠速率的影响与氨基酸性质有关。氨基酸的疏水性可能是折叠动力学的一个重要决定因素，而氨基酸的其他性质，如大小、柔韧性、极性和等电点，对折叠速率常数的贡献很小。
