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Detection of unrelated proteins in sequences multiple alignments by using predicted secondary structures

Authors :
Christophe Geourjon
Mounir Errami
Gilbert Deléage
Institut de biologie et chimie des protéines [Lyon] (IBCP)
Université Claude Bernard Lyon 1 (UCBL)
Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)
Deleage, Gilbert
Source :
Bioinformatics, Bioinformatics, Oxford University Press (OUP), 2003, 19, pp.506-512
Publication Year :
2003
Publisher :
HAL CCSD, 2003.

Abstract

International audience; MOTIVATION: Multiple sequence alignments are essential tools for establishing the homology relations between proteins. Essential amino acids for the function and/or the structure are generally conserved, thus providing key arguments to help in protein characterization. However for distant proteins, it is more difficult to establish, in a reliable way, the homology relations that may exist between them. In this article, we show that secondary structure prediction is a valuable way to validate protein families at low identity rate. RESULTS: We show that the analysis of the secondary structures compatibility is a reliable way to discard non-related proteins in low identity multiple alignment. AVAILABILITY: This validation is possible through our NPS@ server (http://npsa-pbil.ibcp.fr)MOTIVATION: Multiple sequence alignments are essential tools for establishing the homology relations between proteins. Essential amino acids for the function and/or the structure are generally conserved, thus providing key arguments to help in protein characterization. However for distant proteins, it is more difficult to establish, in a reliable way, the homology relations that may exist between them. In this article, we show that secondary structure prediction is a valuable way to validate protein families at low identity rate. RESULTS: We show that the analysis of the secondary structures compatibility is a reliable way to discard non-related proteins in low identity multiple alignment. AVAILABILITY: This validation is possible through our NPS@ server (http://npsa-pbil.ibcp.fr)

Details

Language :
English
ISSN :
13674803 and 13674811
Database :
OpenAIRE
Journal :
Bioinformatics, Bioinformatics, Oxford University Press (OUP), 2003, 19, pp.506-512
Accession number :
edsair.doi.dedup.....6a802da70858a72ca31c0363e1b3874e