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1.
J Theor Biol ; 462: 329-346, 2019 02 07.
Artículo en Inglés | MEDLINE | ID: mdl-30452960

RESUMEN

Research on protein-protein interactions (PPIs) not only helps to reveal the nature of life activities but also plays a driving role in understanding the mechanisms of disease activity and the development of effective drugs. The rapid development of machine learning provides new opportunities and challenges for understanding the mechanism of PPIs. It plays an important role in the field of proteomics research. In recent years, an increasing number of computational methods for predicting PPIs have been developed. This paper proposes a new method for predicting PPIs based on multi-information fusion. First, the pseudo-amino acid composition (PseAAC), auto-covariance (AC) and encoding based on grouped weight (EBGW) methods are used to extract the features of protein sequences, and the extracted three groups of feature vectors were fused. Secondly, the fused feature vectors are denoised by two-dimensional (2-D) wavelet denoising. Finally, the denoised feature vectors are input to the support vector machine (SVM) classifier to predict the PPIs. The ACC of PPIs of Helicobacter pylori (H. pylori) and Saccharomyces cerevisiae (S. cerevisiae) datasets were 95.97% and 95.55% by 5-fold cross-validation test and compared with other prediction methods. The experimental results show that the proposed multi-information fusion prediction method can effectively improve the prediction performance of PPIs. The source code and all datasets are available at https://github.com/QUST-AIBBDRC/PPIs-WDSVM/.


Asunto(s)
Biología Computacional/métodos , Mapeo de Interacción de Proteínas/métodos , Secuencia de Aminoácidos , Aminoácidos , Conjuntos de Datos como Asunto , Helicobacter pylori/química , Saccharomyces cerevisiae/química , Máquina de Vectores de Soporte
2.
J Theor Biol ; 450: 86-103, 2018 08 07.
Artículo en Inglés | MEDLINE | ID: mdl-29678694

RESUMEN

Mitochondrion is important organelle of most eukaryotes and play an important role in participating in various life activities of cells. However, some functions of mitochondria can only be achieved in specific submitochondrial location, the study of submitochondrial locations will help to further understand the biological function of protein, which is a hotspot in proteomics research. In this paper, we propose a new method for protein submitochondrial locations prediction. Firstly, the features of protein sequence are extracted by combining Chou's pseudo-amino acid composition (PseAAC) and pseudo-position specific scoring matrix (PsePSSM). Then the extracted feature information is denoised by two-dimensional (2-D) wavelet denoising. Finally, the optimal feature vectors are input to the SVM classifier to predict the protein submitochondrial locations. We obtained the ideal prediction results by jackknife test and compared with other prediction methods. The results indicate that the proposed method is significantly better than the existing research results, which can provide a new method to predict protein locations in other organelles. The source code and all datasets are available at https://github.com/QUST-BSBRC/PseAAC-PsePSSM-WD/ for academic use.


Asunto(s)
Secuencia de Aminoácidos , Mitocondrias/metabolismo , Posición Específica de Matrices de Puntuación , Proteínas/metabolismo , Algoritmos , Biología Computacional/métodos , Proteínas/fisiología , Proteómica , Máquina de Vectores de Soporte
3.
J Mol Graph Model ; 76: 260-273, 2017 09.
Artículo en Inglés | MEDLINE | ID: mdl-28743071

RESUMEN

Prediction of protein structural class plays an important role in protein structure and function analysis, drug design and many other biological applications. Prediction of protein structural class for low-similarity sequences is still a challenging task. Based on the theory of wavelet denoising, this paper presents a novel method of prediction of protein structural class for the first time. Firstly, the features of the protein sequence are extracted by using Chou's pseudo amino acid composition (PseAAC). Then the extracted feature information is denoised by two-dimensional (2D) wavelet. Finally, the optimal feature vectors are input to support vector machine (SVM) classifier to predict protein structural classes. We obtained significant predictive results using jackknife test on three low-similarity protein structural class datasets 25PDB, 1189 and 640, and compared our method with previous methods The results indicate that the method proposed in this paper can effectively improve the prediction accuracy of protein structural class, which will be a reliable tool for prediction of protein structural class, especially for low-similarity sequences.


Asunto(s)
Aminoácidos/química , Modelos Moleculares , Conformación Proteica , Proteínas/química , Algoritmos , Secuencia de Aminoácidos , Bases de Datos de Proteínas , Curva ROC , Reproducibilidad de los Resultados , Relación Estructura-Actividad , Máquina de Vectores de Soporte
4.
Oncotarget ; 8(64): 107640-107665, 2017 Dec 08.
Artículo en Inglés | MEDLINE | ID: mdl-29296195

RESUMEN

Apoptosis proteins subcellular localization information are very important for understanding the mechanism of programmed cell death and the development of drugs. The prediction of subcellular localization of an apoptosis protein is still a challenging task because the prediction of apoptosis proteins subcellular localization can help to understand their function and the role of metabolic processes. In this paper, we propose a novel method for protein subcellular localization prediction. Firstly, the features of the protein sequence are extracted by combining Chou's pseudo amino acid composition (PseAAC) and pseudo-position specific scoring matrix (PsePSSM), then the feature information of the extracted is denoised by two-dimensional (2-D) wavelet denoising. Finally, the optimal feature vectors are input to the SVM classifier to predict subcellular location of apoptosis proteins. Quite promising predictions are obtained using the jackknife test on three widely used datasets and compared with other state-of-the-art methods. The results indicate that the method proposed in this paper can remarkably improve the prediction accuracy of apoptosis protein subcellular localization, which will be a supplementary tool for future proteomics research.

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