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Impact of Multi-Factor Features on Protein Secondary Structure Prediction.

Authors :
Dong B
Liu Z
Xu D
Hou C
Niu N
Wang G
Source :
Biomolecules [Biomolecules] 2024 Sep 13; Vol. 14 (9). Date of Electronic Publication: 2024 Sep 13.
Publication Year :
2024

Abstract

Protein secondary structure prediction (PSSP) plays a crucial role in resolving protein functions and properties. Significant progress has been made in this field in recent years, and the use of a variety of protein-related features, including amino acid sequences, position-specific score matrices (PSSM), amino acid properties, and secondary structure trend factors, to improve prediction accuracy is an important technical route for it. However, a comprehensive evaluation of the impact of these factor features in secondary structure prediction is lacking in the current work. This study quantitatively analyzes the impact of several major factors on secondary structure prediction models using a more explanatory four-class machine learning approach. The applicability of each factor in the different types of methods, the extent to which the different methods work on each factor, and the evaluation of the effect of multi-factor combinations are explored in detail. Through experiments and analyses, it was found that PSSM performs best in methods with strong high-dimensional features and complex feature extraction capabilities, while amino acid sequences, although performing poorly overall, perform relatively well in methods with strong linear processing capabilities. Also, the combination of amino acid properties and trend factors significantly improved the prediction performance. This study provides empirical evidence for future researchers to optimize multi-factor feature combinations and apply them to protein secondary structure prediction models, which is beneficial in further optimizing the use of these factors to enhance the performance of protein secondary structure prediction models.

Details

Language :
English
ISSN :
2218-273X
Volume :
14
Issue :
9
Database :
MEDLINE
Journal :
Biomolecules
Publication Type :
Academic Journal
Accession number :
39334921
Full Text :
https://doi.org/10.3390/biom14091155