Abstract: The γ-turns play important roles in protein folding and
molecular recognition. The prediction and analysis of γ-turn types are
important for both protein structure predictions and better
understanding the characteristics of different γ-turn types. This study
proposed a physicochemical property-based decision tree (PPDT)
method to interpretably predict γ-turn types. In addition to the good
prediction performance of PPDT, three simple and human
interpretable IF-THEN rules are extracted from the decision tree
constructed by PPDT. The identified informative physicochemical
properties and concise rules provide a simple way for discriminating
and understanding γ-turn types.
Abstract: Protein 3D structure prediction has always been an
important research area in bioinformatics. In particular, the
prediction of secondary structure has been a well-studied research
topic. Despite the recent breakthrough of combining multiple
sequence alignment information and artificial intelligence algorithms
to predict protein secondary structure, the Q3 accuracy of various
computational prediction algorithms rarely has exceeded 75%. In a
previous paper [1], this research team presented a rule-based method
called RT-RICO (Relaxed Threshold Rule Induction from Coverings)
to predict protein secondary structure. The average Q3 accuracy on
the sample datasets using RT-RICO was 80.3%, an improvement
over comparable computational methods. Although this demonstrated
that RT-RICO might be a promising approach for predicting
secondary structure, the algorithm-s computational complexity and
program running time limited its use. Herein a parallelized
implementation of a slightly modified RT-RICO approach is
presented. This new version of the algorithm facilitated the testing of
a much larger dataset of 396 protein domains [2]. Parallelized RTRICO
achieved a Q3 score of 74.6%, which is higher than the
consensus prediction accuracy of 72.9% that was achieved for the
same test dataset by a combination of four secondary structure
prediction methods [2].