Protein is an essential component of the living organism. The prediction of protein-protein interactions (PPIs) has important implications for understanding the behavioral processes of life, preventing diseases, and developing new drugs. Although the development of high-throughput technology makes it possible to identify PPIs in large-scale biological experiments, it restricts the extensive use of experimental methods due to the constraints of time, cost, false positive rate and other conditions. Therefore, there is an urgent need for computational methods as a supplement to experimental methods to predict PPIs rapidly and accurately. In this paper, we propose a novel approach, namely CNN-FSRF, for predicting PPIs based on protein sequence by combining deep learning Convolution Neural Network (CNN) with Feature-Selective Rotation Forest (FSRF). The proposed method firstly converts the protein sequence into the Position-Specific Scoring Matrix (PSSM) containing biological evolution information, then uses CNN to objectively and efficiently extracts the deeply hidden features of the protein, and finally removes the redundant noise information by FSRF and gives the accurate prediction results. When performed on the PPIs datasets Yeast and Helicobacter pylori, CNN-FSRF achieved a prediction accuracy of 97.75% and 88.96%. To further evaluate the prediction performance, we compared CNN-FSRF with SVM and other existing methods. In addition, we also verified the performance of CNN-FSRF on independent datasets. Excellent experimental results indicate that CNN-FSRF can be used as a useful complement to biological experiments to identify protein interactions.
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http://dx.doi.org/10.1038/s41598-019-46369-4 | DOI Listing |
Am J Hum Genet
January 2025
Department of Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
Each human genome has approximately 5 million DNA variants. Even for complete loss-of-function variants causing inherited, monogenic diseases, current understanding based on gene-specific molecular function does not adequately predict variability observed between people with identical mutations or fluctuating disease trajectories. We present a parallel paradigm for loss-of-function variants based on broader consequences to the cell when aberrant polypeptide chains of amino acids are translated from mutant RNA to generate mutated proteins.
View Article and Find Full Text PDFBiophys Chem
December 2024
Theoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; Computational Biophysics Research Group, RIKEN Center for Computational Science, 7-1-26 Minatojima-Minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan; Laboratory for Biomolecular Function Simulation, RIKEN Center for Biosystems Dynamics Research, 1-6-5 Minatojima-Minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan.
Membrane potential is essential in biological signaling and homeostasis maintained by voltage-sensitive membrane proteins. Molecular dynamics (MD) simulations incorporating membrane potentials have been extensively used to study the structures and functions of ion channels and protein pores. They can also be beneficial in designing and characterizing artificial ion channels and pores, which will guide further amino acid sequence optimization through comparison between the predicted models and experimental data.
View Article and Find Full Text PDFFEBS J
January 2025
Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Rhizobium etli is a nitrogen-fixing bacterium that encodes two l-asparaginases. The structure of the inducible R. etli asparaginase ReAV has been recently determined to reveal a protein with no similarity to known enzymes with l-asparaginase activity, but showing a curious resemblance to glutaminases and β-lactamases.
View Article and Find Full Text PDFBMC Plant Biol
January 2025
Institute of Tropical Horticulture Research, Hainan Academy of Agricultural Sciences, Haikou, 571100, China.
Background: Tea-oil Camellia within the genus Camellia is renowned for its premium Camellia oil, often described as "Oriental olive oil". So far, only one partial mitochondrial genomes of Tea-oil Camellia have been published (no main Tea-oil Camellia cultivars), and comparative mitochondrial genomic studies of Camellia remain limited.
Results: In this study, we first reconstructed the entire mitochondrial genome of C.
J Proteome Res
January 2025
Department of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.
Proteo-SAFARI is a shiny application for fragment assignment by relative isotopes, an R-based software application designed for identification of protein fragment ions directly in the / domain. This program provides an open-source, user-friendly application for identification of fragment ions from a candidate protein sequence with support for custom covalent modifications and various visualizations of identified fragments. Additionally, Proteo-SAFARI includes a nonnegative least-squares fitting approach to determine the contributions of various hydrogen shifted fragment ions ( + 1, + 1, - 1, - 2) observed in UVPD mass spectra which exhibit overlapping isotopic distributions.
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