Related Experiment Video
Updated: Jun 19, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Prediction of interactiveness of proteins and nucleic acids based on feature selections
YouLang Yuan1, XiaoHe Shi, XinLei Li
1Chemical Data mining Laboratory, Department of Chemistry, College of Sciences, Shanghai University, 99 Shang-Da Road, Shanghai, 200444, People's Republic of China.
Abstract:
It is important to identify which proteins can interact with nucleic acids for the purpose of protein annotation, since interactions between nucleic acids and proteins involve in numerous cellular processes such as replication, transcription, splicing, and DNA repair. This research tries to identify proteins that can interact with DNA, RNA, and rRNA, respectively. mRMR (Minimum redundancy and maximum relevance), with its elegant mathematical formulation, has been applied widely in processing biological data and feature analysis since its introduction in 2005. mRMR plus incremental feature selection (IFS) is known to be very efficient in feature selection and analysis, and able to improve both effectiveness and efficiency of a prediction model. IFS is applied to decide how many features should be selected from feature list provided by mRMR. In the end, the selected features of mRMR and IFS are further refined by a conventional feature selection method--forward feature wrapper (FFW), by reordering the features. Each protein is coded by 132 features including amino acid compositions and physicochemical properties. After the feature selection, k-Nearest Neighbor algorithm, the adopted prediction model, is trained and tested. As a result, the optimized prediction accuracies for the DNA, RNA, and rRNA are 82.0, 83.4, and 92.3%, respectively. Furthermore, the most important features that contribute to the prediction are identified and analyzed biologically. The predictor, developed for this research, is available for public access at http://chemdata.shu.edu.cn/protein_na_mrmr/.
Related Concept Videos
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces
Protein-Protein Interfaces
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

