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Updated: Sep 21, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
A Novel Ensemble Learning-Based Computational Method to Predict Protein-Protein Interactions from Protein Primary
Jie Pan1, Shiwei Wang1, Changqing Yu2
1Key Laboratory of Resources Biology and Biotechnology in Western China, Ministry of Education, College of Life Science, Northwest University, Xi'an 710069, China.
Abstract:
Protein-protein interactions (PPIs) are crucial for understanding the cellular processes, including signal cascade, DNA transcription, metabolic cycles, and repair. In the past decade, a multitude of high-throughput methods have been introduced to detect PPIs. However, these techniques are time-consuming, laborious, and always suffer from high false negative rates. Therefore, there is a great need of new computational methods as a supplemental tool for PPIs prediction. In this article, we present a novel sequence-based model to predict PPIs that combines Discrete Hilbert transform (DHT) and Rotation Forest (RoF). This method contains three stages: firstly, the Position-Specific Scoring Matrices (PSSM) was adopted to transform the amino acid sequence into a PSSM matrix, which can contain rich information about protein evolution. Then, the 400-dimensional DHT descriptor was constructed for each protein pair. Finally, these feature descriptors were fed to the RoF classifier for identifying the potential PPI class. When exploring the proposed model on the Yeast, Human, and Oryza sativa PPIs datasets, it yielded excellent prediction accuracies of 91.93, 96.35, and 94.24%, respectively. In addition, we also conducted numerous experiments on cross-species PPIs datasets, and the predictive capacity of our method is also very excellent. To further access the prediction ability of the proposed approach, we present the comparison of RoF with four powerful classifiers, including Support Vector Machine (SVM), Random Forest (RF), K-nearest Neighbor (KNN), and AdaBoost. We also compared it with some existing superiority works. These comprehensive experimental results further confirm the excellent and feasibility of the proposed approach. In future work, we hope it can be a supplemental tool for the proteomics analysis.
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