Abstract
Introduction: The primary structure of the protein is a polypeptide chain made up of a sequence of amino acids. What happens due to interaction between the atoms of the backbone is that it forms within a polypeptide folded structure, which is very much within the secondary structure. These alignments can be made more accurate by the inclusion of secondary structure information. Objective: It is difficult to identify the sequence information embedded in the secondary structure of the protein. However, Deep learning methods can be used for solving the identification of the sequence information in the protein structures. Methods: The scope of the proposed work is to increase the accuracy of identifying the sequence information in the primary structure and the tertiary structure, thereby increasing the accuracy of the predicted Protein Secondary Structure (PSS). In this proposed work, homology is eliminated by a Recurrent Neural Network (RNN) based network that consists of three layers, namely bi-directional Long Short Term Memory (LSTM), time distributed layer and Softmax layer. Results: The proposed LDS model achieves an accuracy of approximately 86% for the prediction of the three-state secondary structure of the protein. Conclusion: The gap between the number of protein primary structures and secondary structures is huge and increasing. Machine learning is trying to reduce this gap. In most of the other pre attempts in predicting the secondary structure of proteins, the data is divided according to the homology of the proteins. This limits the efficiency of the predicting model and the inputs given to such models. Hence, in our model, homology has not been considered while collecting the data for training or testing out model. This has led to our model to not be affected by the homology of the protein fed to it and hence remove that restriction, so any protein can be fed to it.
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