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DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification

DiANNA is a recent state-of-the-art artificial neural network and web server, which determines the cysteine oxidation state and disulfide connectivity of a protein, given only its amino acid sequence. Version 1.0 of DiANNA uses a feed-forward neural network to determine which cysteines are involved...

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Detalles Bibliográficos
Autores principales: Ferrè, F., Clote, P.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1538812/
https://www.ncbi.nlm.nih.gov/pubmed/16844987
http://dx.doi.org/10.1093/nar/gkl189
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author Ferrè, F.
Clote, P.
author_facet Ferrè, F.
Clote, P.
author_sort Ferrè, F.
collection PubMed
description DiANNA is a recent state-of-the-art artificial neural network and web server, which determines the cysteine oxidation state and disulfide connectivity of a protein, given only its amino acid sequence. Version 1.0 of DiANNA uses a feed-forward neural network to determine which cysteines are involved in a disulfide bond, and employs a novel architecture neural network to predict which half-cystines are covalently bound to which other half-cystines. In version 1.1 of DiANNA, described here, we extend functionality by applying a support vector machine with spectrum kernel for the cysteine classification problem—to determine whether a cysteine is reduced (free in sulfhydryl state), half-cystine (involved in a disulfide bond) or bound to a metallic ligand. In the latter case, DiANNA predicts the ligand among iron, zinc, cadmium and carbon. Available at: .
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spelling pubmed-15388122006-08-18 DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification Ferrè, F. Clote, P. Nucleic Acids Res Article DiANNA is a recent state-of-the-art artificial neural network and web server, which determines the cysteine oxidation state and disulfide connectivity of a protein, given only its amino acid sequence. Version 1.0 of DiANNA uses a feed-forward neural network to determine which cysteines are involved in a disulfide bond, and employs a novel architecture neural network to predict which half-cystines are covalently bound to which other half-cystines. In version 1.1 of DiANNA, described here, we extend functionality by applying a support vector machine with spectrum kernel for the cysteine classification problem—to determine whether a cysteine is reduced (free in sulfhydryl state), half-cystine (involved in a disulfide bond) or bound to a metallic ligand. In the latter case, DiANNA predicts the ligand among iron, zinc, cadmium and carbon. Available at: . Oxford University Press 2006-07-01 2006-07-14 /pmc/articles/PMC1538812/ /pubmed/16844987 http://dx.doi.org/10.1093/nar/gkl189 Text en © The Author 2006. Published by Oxford University Press. All rights reserved
spellingShingle Article
Ferrè, F.
Clote, P.
DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification
title DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification
title_full DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification
title_fullStr DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification
title_full_unstemmed DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification
title_short DiANNA 1.1: an extension of the DiANNA web server for ternary cysteine classification
title_sort dianna 1.1: an extension of the dianna web server for ternary cysteine classification
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1538812/
https://www.ncbi.nlm.nih.gov/pubmed/16844987
http://dx.doi.org/10.1093/nar/gkl189
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