Detalhes bibliográficos
| Ano de defesa: |
2023 |
| Autor(a) principal: |
Almeida, Alexandre Barbosa de
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| Orientador(a): |
Soares, Telma Woerle de Lima
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| Banca de defesa: |
Soares , Telma Woerle de Lima,
Camilo Junior , Celso Gonoalves,
Vieira, Flávio Henrique Teles,
Delbem, Alexandre Cláudio Botazzo,
Faccioli, Rodrigo Antônio |
| Tipo de documento: |
Tese
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| Tipo de acesso: |
Acesso aberto |
| Idioma: |
por |
| Instituição de defesa: |
Universidade Federal de Goiás
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| Programa de Pós-Graduação: |
Programa de Pós-graduação em Ciência da Computação (INF)
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| Departamento: |
Instituto de Informática - INF (RG)
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| País: |
Brasil
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| Palavras-chave em Português: |
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| Palavras-chave em Inglês: |
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| Área do conhecimento CNPq: |
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| Link de acesso: |
http://repositorio.bc.ufg.br/tede/handle/tede/13057
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Resumo: |
Proteins are organic molecules composed of chains of amino acids and play a variety of essential biological functions in the body. The native structure of a protein is the result of the folding process of its amino acids, with their spatial orientation primarily determined by two dihedral angles (φ, ψ). This work proposes a new hybrid method for predicting the tertiary structures of proteins called hyPROT, combining techniques of Multi-objective Evolutionary Algorithm optimization (MOEA), Molecular Dynamics, and Recurrent Neural Networks (RNNs). The proposed approach investigates the evolutionary profile of dihedral angles (φ, ψ) obtained by different MOEAs during the minimization process of the objective function by dominance and energy minimization by molecular dynamics. This proposal is unprecedented in the protein prediction literature. The premise under investigation is that the evolutionary profile of dihedrals may be concealing relevant patterns about folding mechanisms. To analyze the evolutionary profile of angles (φ, ψ), RNNs were used to abstract and generalize the specific biases of each MOEA. The selected MOEAs were NSGAII, BRKGA, and GDE3, and the objective function investigated combines the potential energy from non-covalent interactions and the solvation energy. The results obtained show that the hyPROT was able to reduce the RMSD value of the best prediction generated by the MOEAs individually by at least 33%. Predicting new series for dihedral angles allowed for the formation of histograms, indicating the formation of a possible statistical ensemble responsible for the distribution of dihedrals (φ, ψ) during the folding process |
