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Convolutional neural networks (CNNs) are currently among the most widely-used deep neural network (DNN) architectures available and achieve state-of-the-art performance for many problems. Originally applied to computer vision tasks, CNNs work well with any data with a spatial relationship, besides images, and have been applied to different fields. However, recent works have highlighted numerical stability challenges in DNNs, which also relates to their known sensitivity to noise injection. These challenges can jeopardise their performance and reliability. This paper investigates DeepGOPlus, a CNN that predicts protein function. DeepGOPlus has achieved state-of-the-art performance and can successfully take advantage and annotate the abounding protein sequences emerging in proteomics. We determine the numerical stability of the model's inference stage by quantifying the numerical uncertainty resulting from perturbations of the underlying floating-point data. In addition, we explore the opportunity to use reduced-precision floating point formats for DeepGOPlus inference, to reduce memory consumption and latency. This is achieved by instrumenting DeepGOPlus' execution using Monte Carlo Arithmetic, a technique that experimentally quantifies floating point operation errors and VPREC, a tool that emulates results with customizable floating point precision formats. Focus is placed on the inference stage as it is the primary deliverable of the DeepGOPlus model, widely applicable across different environments. All in all, our results show that although the DeepGOPlus CNN is very stable numerically, it can only be selectively implemented with lower-precision floating-point formats. We conclude that predictions obtained from the pre-trained DeepGOPlus model are very reliable numerically, and use existing floating-point formats efficiently. [ABSTRACT FROM AUTHOR]

Protein hotspot residues are key sites that mediate protein-protein interactions. Accurate identification of these residues is essential for understanding the mechanism from protein to function and for designing drug targets. Current research has mostly focused on using machine learning methods to predict hot spots from known interface residues, which artificially extract the corresponding features of amino acid residues from sequence, structure, evolution, energy, and other information to train and test machine learning models. The process is cumbersome, time-consuming and laborious to some extent. This paper proposes a novel idea that develops a pre-trained protein sequence embedding model combined with a one-dimensional convolutional neural network, called Embed-1dCNN, to predict protein hotspot residues. In order to obtain large data samples, this work integrates and extracts data from the datasets of ASEdb, BID, SKEMPI and dbMPIKT to generate a new dataset, and adopts the SMOTE algorithm to expand positive samples to form the training set. The experimental results show that the method achieves an F1 score of 0.82 on the test set. Compared with other hot spot prediction methods, our model achieved better prediction performance. [ABSTRACT FROM AUTHOR]

Protein secondary structure prediction is extremely important for determining the spatial structure and function of proteins. In this paper, we apply an optimized convolutional neural network and long short-term memory neural network models to protein secondary structure prediction, which is called OCLSTM. We use an optimized convolutional neural network to extract local features between amino acid residues. Then use the bidirectional long short-term memory neural network to extract the remote interactions between the internal residues of the protein sequence to predict the protein structure. Experiments are performed on CASP10, CASP11, CASP12, CB513, and 25PDB datasets, and the good performance of 84.68%, 82.36%, 82.91%, 84.21% and 85.08% is achieved respectively. Experimental results show that the model can achieve better results. [ABSTRACT FROM AUTHOR]

Proteins are fundamental components of diverse cellular systems and play crucial roles in a variety of disease processes. Consequently, it is crucial to comprehend their structure, function, and intricate interconnections. Classifying proteins into families or groups with comparable structural and functional characteristics is a crucial aspect of this comprehension. This classification is crucial for evolutionary research, predicting protein function, and identifying potential therapeutic targets. Sequence alignment and structure-based alignment are frequently ineffective techniques for identifying protein families.This study addresses the need for a more efficient and accurate technique for feature extraction and protein classification. The research proposes a novel method that integrates bispectrum characteristics, deep learning techniques, and machine learning algorithms to overcome the limitations of conventional methods. The proposed method uses numbers to represent protein sequences, utilizes bispectrum analysis, uses different topologies for convolutional neural networks to pull out features, and chooses robust features to classify protein families. The goal is to outperform existing methods for identifying protein families, thereby enhancing classification metrics. The materials consist of numerous protein datasets, whereas the methods incorporate bispectrum characteristics and deep learning strategies. The results of this study demonstrate that the proposed method for identifying protein families is superior to conventional approaches. Significantly enhanced quality metrics demonstrated the efficacy of the combined bispectrum and deep learning approaches. These findings have the potential to advance the field of protein biology and facilitate pharmaceutical innovation. In conclusion, this study presents a novel method that employs bispectrum characteristics and deep learning techniques to improve the precision and efficiency of protein family identification. The demonstrated advancements in classification metrics demonstrate this method's applicability to numerous scientific disciplines. This furthers our understanding of protein function and its implications for disease and treatment. [ABSTRACT FROM AUTHOR]

Plasmodium falciparum is a parasitic protozoan that can cause malaria, which is a deadly disease. Therefore, the accurate identification of malaria parasite mitochondrial proteins is essential for understanding their functions and identifying novel drug targets. For classifying protein sequences, several adaptive statistical techniques have been devised. Despite significant gains, prediction performance is still constrained by the lack of appropriate feature descriptors and learning strategies in current systems. Moreover, good ground truth data is important for Artificial Intelligence (AI)-based models but there is a lack of that data in the literature. Therefore, in this work, we propose a novel hybrid network that combines 1D Convolutional Neural Network (CNN) and Bidirectional Gated Recurrent Unit (BGRU) to classify the malaria parasite mitochondrial proteins. Furthermore, we curate a sequential data that are collected from National Center for Biotechnology Information (NCBI) and UniProtKB/Swiss-Prot proteins databanks to prepare a dataset that can be used by the research community for AI-based algorithms evaluation. We obtain 4204 cases after preprocessing of the collected data and denote this set of proteins as PF4204. Finally, we conduct an ablation study on several conventional and deep models using PF4204 and the benchmark PF2095 datasets. The proposed model 'CNN-BGRU' obtains the accuracy values of 0.9096 and 0.9857 on PF4204 and PF2095 datasets, respectively. In addition, the CNN-BGRU is compared with state-of-the-arts, where the results illustrate that it can extract robust features and identify proteins accurately. [ABSTRACT FROM AUTHOR]