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A multi-objective optimization approach accurately resolves protein domain architectures

Motivation: Given a protein sequence and a number of potential domains matching it, what are the domain content and the most likely domain architecture for the sequence? This problem is of fundamental importance in protein annotation, constituting one of the main steps of all predictive annotation s...

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Autores principales: Bernardes, J.S., Vieira, F.R.J., Zaverucha, G., Carbone, A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4734041/
https://www.ncbi.nlm.nih.gov/pubmed/26458889
http://dx.doi.org/10.1093/bioinformatics/btv582
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author Bernardes, J.S.
Vieira, F.R.J.
Zaverucha, G.
Carbone, A.
author_facet Bernardes, J.S.
Vieira, F.R.J.
Zaverucha, G.
Carbone, A.
author_sort Bernardes, J.S.
collection PubMed
description Motivation: Given a protein sequence and a number of potential domains matching it, what are the domain content and the most likely domain architecture for the sequence? This problem is of fundamental importance in protein annotation, constituting one of the main steps of all predictive annotation strategies. On the other hand, when potential domains are several and in conflict because of overlapping domain boundaries, finding a solution for the problem might become difficult. An accurate prediction of the domain architecture of a multi-domain protein provides important information for function prediction, comparative genomics and molecular evolution. Results: We developed DAMA (Domain Annotation by a Multi-objective Approach), a novel approach that identifies architectures through a multi-objective optimization algorithm combining scores of domain matches, previously observed multi-domain co-occurrence and domain overlapping. DAMA has been validated on a known benchmark dataset based on CATH structural domain assignments and on the set of Plasmodium falciparum proteins. When compared with existing tools on both datasets, it outperforms all of them. Availability and implementation: DAMA software is implemented in C++ and the source code can be found at http://www.lcqb.upmc.fr/DAMA. Contact: juliana.silva_bernardes@upmc.fr or alessandra.carbone@lip6.fr Supplementary information: Supplementary data are available at Bioinformatics online.
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spelling pubmed-47340412016-02-02 A multi-objective optimization approach accurately resolves protein domain architectures Bernardes, J.S. Vieira, F.R.J. Zaverucha, G. Carbone, A. Bioinformatics Original Papers Motivation: Given a protein sequence and a number of potential domains matching it, what are the domain content and the most likely domain architecture for the sequence? This problem is of fundamental importance in protein annotation, constituting one of the main steps of all predictive annotation strategies. On the other hand, when potential domains are several and in conflict because of overlapping domain boundaries, finding a solution for the problem might become difficult. An accurate prediction of the domain architecture of a multi-domain protein provides important information for function prediction, comparative genomics and molecular evolution. Results: We developed DAMA (Domain Annotation by a Multi-objective Approach), a novel approach that identifies architectures through a multi-objective optimization algorithm combining scores of domain matches, previously observed multi-domain co-occurrence and domain overlapping. DAMA has been validated on a known benchmark dataset based on CATH structural domain assignments and on the set of Plasmodium falciparum proteins. When compared with existing tools on both datasets, it outperforms all of them. Availability and implementation: DAMA software is implemented in C++ and the source code can be found at http://www.lcqb.upmc.fr/DAMA. Contact: juliana.silva_bernardes@upmc.fr or alessandra.carbone@lip6.fr Supplementary information: Supplementary data are available at Bioinformatics online. Oxford University Press 2016-02-01 2015-10-12 /pmc/articles/PMC4734041/ /pubmed/26458889 http://dx.doi.org/10.1093/bioinformatics/btv582 Text en © The Author 2015. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Original Papers
Bernardes, J.S.
Vieira, F.R.J.
Zaverucha, G.
Carbone, A.
A multi-objective optimization approach accurately resolves protein domain architectures
title A multi-objective optimization approach accurately resolves protein domain architectures
title_full A multi-objective optimization approach accurately resolves protein domain architectures
title_fullStr A multi-objective optimization approach accurately resolves protein domain architectures
title_full_unstemmed A multi-objective optimization approach accurately resolves protein domain architectures
title_short A multi-objective optimization approach accurately resolves protein domain architectures
title_sort multi-objective optimization approach accurately resolves protein domain architectures
topic Original Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4734041/
https://www.ncbi.nlm.nih.gov/pubmed/26458889
http://dx.doi.org/10.1093/bioinformatics/btv582
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