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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
16/02/2009 |
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Data da última atualização: |
15/01/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
HIGA, R. H.; TOZZI, C. L. |
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Afiliação: |
ROBERTO HIROSHI HIGA, CNPTIA; CLESIO LUIS TOZZI, UNICAMP. |
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Título: |
A simple and efficient method for predicting protein-protein interaction sites. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
Genetics and Molecular Research, v. 7, n. 3, p. 898-909, 2008. |
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Idioma: |
Inglês |
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Conteúdo: |
Computational methods for predicting protein-protein interaction sites based on structural data are characterized by an accuracy between 70 and 80%. Some experimental studies indicate that only a fraction of the residues, forming clusters in the center of the interaction site, are energetically important for binding. In addition, the analysis of amino acid composition has shown that residues located in the center of the interaction site can be better discriminated from the residues in other parts of the protein surface. In the present study, we implement a simple method to predict interaction site residues exploiting this fact and show that it achieves a very competitive performance compared to other methods using the same dataset and criteria for performance evaluation (success rate of 82.1%). |
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Palavras-Chave: |
Estrutura da proteína; Previsão de sítios de interação; Previsão de sítios de ligação; Sítios de interação; Sítios de ligação. |
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Thesagro: |
Genética; Proteína. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/158354/1/SIMPLE.pdf
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Marc: |
LEADER 01489naa a2200217 a 4500
001 1024589
005 2020-01-15
008 2008 bl uuuu u00u1 u #d
100 1 $aHIGA, R. H.
245 $aA simple and efficient method for predicting protein-protein interaction sites.$h[electronic resource]
260 $c2008
520 $aComputational methods for predicting protein-protein interaction sites based on structural data are characterized by an accuracy between 70 and 80%. Some experimental studies indicate that only a fraction of the residues, forming clusters in the center of the interaction site, are energetically important for binding. In addition, the analysis of amino acid composition has shown that residues located in the center of the interaction site can be better discriminated from the residues in other parts of the protein surface. In the present study, we implement a simple method to predict interaction site residues exploiting this fact and show that it achieves a very competitive performance compared to other methods using the same dataset and criteria for performance evaluation (success rate of 82.1%).
650 $aGenética
650 $aProteína
653 $aEstrutura da proteína
653 $aPrevisão de sítios de interação
653 $aPrevisão de sítios de ligação
653 $aSítios de interação
653 $aSítios de ligação
700 1 $aTOZZI, C. L.
773 $tGenetics and Molecular Research$gv. 7, n. 3, p. 898-909, 2008.
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Embrapa Agricultura Digital (CNPTIA) |
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