Several properties of amino acid sequences corresponding to proteins that are known to fold are compared to those of randomly generated sequences and to sequences of intrinsically disordered proteins in order to find properties that distinguish folding sequences from the rest. The properties studied included helix and sheet propensities from secondary structure prediction, adjacency correlations, directionality correlations, as well as propensities of all possible triplets and quadruplets. Small differences between known folded and random sequences were observed for the adjacency and directional correlations, and significant differences were seen on the triplet and especially on the quadruplet propensities. Based on the differences in the adjacency, triplet or quadruplet propensities folding scores were defined and used to test the accuracy of foldability prediction based on these statistics. The best predictions were obtained from the quadruplet propensities.

中文翻译：

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从其序列预测蛋白质的可折叠性。

将与已知折叠的蛋白质相对应的氨基酸序列的几种特性与随机产生的序列的氨基酸特性和与内在无序的蛋白质的序列的特性进行比较，以找出区分折叠序列与其余序列的特性。研究的特性包括来自二级结构预测的螺旋和片状倾向，邻接相关性，方向性相关性以及所有可能的三连体和四连体的倾向。观察到已知折叠序列和随机序列之间的微小差异，即邻接关系和方向相关性，并且在三联体，尤其是四联体倾向上观察到了显着差异。根据邻接关系的差异，定义了三联体或四联体倾向性折叠得分，并根据这些统计数据测试可折叠性预测的准确性。最佳预测是从四联体倾向中获得的。