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1.
Amino Acids ; 38(4): 1201-8, 2010 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-19653066

RESUMO

Apoptosis proteins have a central role in the development and homeostasis of an organism. These proteins are very important for understanding the mechanism of programmed cell death. As a result of genome and other sequencing projects, the gap between the number of known apoptosis protein sequences and the number of known apoptosis protein structures is widening rapidly. Because of this extremely unbalanced state, it would be worthwhile to develop a fast and reliable method to identify their subcellular locations so as to gain better insight into their biological functions. In view of this, a new method, in which the support vector machine combines with discrete wavelet transform, has been developed to predict the subcellular location of apoptosis proteins. The results obtained by the jackknife test were quite promising, and indicated that the proposed method can remarkably improve the prediction accuracy of subcellular locations, and might also become a useful high-throughput tool in characterizing other attributes of proteins, such as enzyme class, membrane protein type, and nuclear receptor subfamily according to their sequences.


Assuntos
Proteínas Reguladoras de Apoptose/química , Proteínas Reguladoras de Apoptose/metabolismo , Biologia Computacional/métodos , Modelos Biológicos , Análise de Sequência de Proteína/métodos , Sequência de Aminoácidos , Aminoácidos/química , Animais , Proteínas Reguladoras de Apoptose/classificação , Inteligência Artificial , Bases de Dados de Proteínas , Sistemas Inteligentes , Ensaios de Triagem em Larga Escala , Humanos , Interações Hidrofóbicas e Hidrofílicas , Transporte Proteico , Software , Frações Subcelulares/metabolismo
2.
J Comput Chem ; 30(8): 1344-50, 2009 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-19009604

RESUMO

The prediction of secondary structure is a fundamental and important component in the analytical study of protein structure and functions. How to improve the predictive accuracy of protein structural classification by effectively incorporating the sequence-order effects is an important and challenging problem. In this study, a new method, in which the support vector machine combines with discrete wavelet transform, is developed to predict the protein structural classes. Its performance is assessed by cross-validation tests. The predicted results show that the proposed approach can remarkably improve the success rates, and might become a useful tool for predicting the other attributes of proteins as well.


Assuntos
Algoritmos , Proteínas/química , Simulação por Computador , Interações Hidrofóbicas e Hidrofílicas , Modelos Químicos , Conformação Proteica , Estrutura Secundária de Proteína
3.
J Theor Biol ; 256(4): 625-31, 2009 Feb 21.
Artigo em Inglês | MEDLINE | ID: mdl-19049810

RESUMO

The enzymatic attributes of newly found protein sequences are usually determined either by biochemical analysis of eukaryotic and prokaryotic genomes or by microarray chips. These experimental methods are both time-consuming and costly. With the explosion of protein sequences registered in the databanks, it is highly desirable to develop an automated method to identify whether a given new sequence belongs to enzyme or non-enzyme. The discrete wavelet transform (DWT) and support vector machine (SVM) have been used in this study for distinguishing enzyme structures from non-enzymes. The networks have been trained and tested on two datasets of proteins with different wavelet basis functions, decomposition scales and hydrophobicity data types. Maximum accuracy has been obtained using SVM with a wavelet function of Bior2.4, a decomposition scale j=5, and Kyte-Doolittle hydrophobicity scales. The results obtained by the self-consistency test, jackknife test and independent dataset test are encouraging, which indicates that the proposed method can be employed as a useful assistant technique for distinguishing enzymes from non-enzymes.


Assuntos
Enzimas/química , Modelos Químicos , Animais , Inteligência Artificial , Físico-Química , Estudos de Viabilidade , Interações Hidrofóbicas e Hidrofílicas , Proteínas/química
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