Describing the whole story of protein folding is currently the main enigmatic problem in molecular bioinformatics study. Protein folding mechanisms have been intensively investigated with experimental as well as simulation techniques. Since a protein folds into its specific 3D structure from a unique amino acid sequence, it is interesting to extract as much information as possible from the amino acid sequence of a protein. Analyses based on inter-residue average distance statistics and a coarse-grained Gō-model simulation were conducted on Ig and FN3 domains of a titin protein to decode the folding mechanisms from their sequence data and native structure data, respectively. The central region of all domains was predicted to be an initial folding unit, that is, stable in an early state of folding. This common feature coincides well with the experimental results and underscores the significance of the β-sandwich proteins' common structure, namely, the key strands for folding and the Greek-key motif, which is located in the central region. We confirmed that our sequence-based techniques were able to predict the initial folding event just next to the denatured state and that a 3D-based Gō-model simulation can be used to investigate the whole process of protein folding.

中文翻译：

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Ig样β三明治蛋白的初始折叠位点和整个折叠过程的预测。

描述蛋白质折叠的整个过程是当前分子生物信息学研究中的主要难题。蛋白质折叠机制已通过实验和模拟技术进行了深入研究。由于蛋白质从独特的氨基酸序列折叠成特定的3D结构，因此从蛋白质的氨基酸序列中提取尽可能多的信息是很有趣的。基于残基间平均距离统计数据和粗粒Gō模型模拟，对titin蛋白的Ig和FN3域进行了分析，以分别从其序列数据和天然结构数据中解码折叠机制。预测所有域的中心区域都是初始折叠单元，即在折叠的早期状态下是稳定的。这个共同特征与实验结果很好地吻合，并强调了β-三明治蛋白共同结构的重要性，即折叠的关键链和位于中央区域的希腊钥匙基序。我们证实了我们基于序列的技术能够预测接近变性状态的初始折叠事件，并且可以使用基于3D的Gō模型模拟来研究蛋白质折叠的整个过程。