Abstract
Predicting protein-DNA binding sites is a challenging computational problem in the field of bioinformatics. Identifying the specific residues where proteins bind to DNA is of paramount importance, as it enables the modeling of their interactions and facilitates downstream studies. Nevertheless, the development of accurate and efficient computational methods for this task remains a persistent challenge. Accurate prediction of protein-DNA binding sites has far-reaching implications for understanding molecular mechanisms, disease processes, drug discovery, and synthetic biology applications. It helps bridge the gap between genomics and functional biology, enabling researchers to uncover the intricacies of cellular processes and advance our knowledge of the biological world. The method used to predict DNA binding residues in this study is a potent combination of conventional bioinformatics tools, protein language models, and cutting-edge machine learning and deep learning classifiers. On a dataset of protein-DNA binding sites, our model is meticulously trained, and it is then rigorously examined using several experiments. As indicated by higher predictive behavior with AUC values on two benchmark datasets, the results show superior performance when compared to existing models. The suggested model has a strong capacity for generalization and shows specificity for DNA-binding sites. We further demonstrated the adaptability of our model as a universal framework for binding site prediction by training it on a variety of protein-ligand binding site datasets. In conclusion, our innovative approach for predicting protein-DNA binding residues holds great promise in advancing our understanding of molecular interactions, thus paving the way for several groundbreaking applications in the field of molecular biology and genetics. Our approach demonstrated efficacy and versatility underscore its potential for driving transformative discoveries in biomolecular research.
Competing Interest Statement
The authors have declared no competing interest.
Footnotes
tmurad2{at}student.gsu.edu,pchourasia1{at}student.gsu.edu,sali85{at}student.gsu.edu, mpatterson30{at}gsu.edu
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