Prediction of protein secondary structure by the improved TCN-BiLSTM-MHA model with knowledge distillation

Abstract

AbstractSecondary structure prediction is a key step in understanding protein function and biological properties and is highly important in the fields of new drug development, disease treatment, bioengineering, etc. Accurately predicting the secondary structure of proteins helps to reveal how proteins are folded and how they function in cells. The application of deep learning models in protein structure prediction is particularly important because of their ability to process complex sequence information and extract meaningful patterns and features, thus significantly improving the accuracy and efficiency of prediction. In this study, a combined model integrating an improved temporal convolutional network (TCN), bidirectional long short-term memory (BiLSTM), and a multi-head attention (MHA) mechanism is proposed to enhance the accuracy of protein prediction in both eight-state and three-state structures. One-hot encoding features and word vector representations of physicochemical properties are incorporated. A significant emphasis is placed on knowledge distillation techniques utilizing the ProtT5 pretrained model, leading to performance improvements. The improved TCN, achieved through multiscale fusion and bidirectional operations, allows for better extraction of amino acid sequence features than traditional TCN models. The model demonstrated excellent prediction performance on multiple datasets. For the TS115, CB513 and PDB (2018–2020) datasets, the prediction accuracy of the eight-state structure of the six datasets in this paper reached 88.2%, 84.9%, and 95.3%, respectively, and the prediction accuracy of the three-state structure reached 91.3%, 90.3%, and 96.8%, respectively. This study not only improves the accuracy of protein secondary structure prediction but also provides an important tool for understanding protein structure and function, which is particularly applicable to resource-constrained contexts and provides a valuable tool for understanding protein structure and function.