Supersecondary structure prediction of transmembrane beta-barrel proteins.

Van Du T Tran Philippe Chassignet Jean-Marc Steyaert 1, 2
2 AMIB - Algorithms and Models for Integrative Biology
CNRS - Centre National de la Recherche Scientifique : UMR8623, Polytechnique - X, Inria Saclay - Ile de France, UP11 - Université Paris-Sud - Paris 11, LRI - Laboratoire de Recherche en Informatique, LIX - Laboratoire d'informatique de l'École polytechnique [Palaiseau]
Abstract : We introduce a graph-theoretic model for predicting the supersecondary structure of transmembrane β-barrel proteins--a particular class of proteins that performs diverse important functions but it is difficult to determine their structure with experimental methods. This ab initio model resolves the protein folding problem based on pseudo-energy minimization with the aid of a simple probabilistic filter. It also allows for determining structures whose barrel follows a given permutation on the arrangement of β-strands, and allows for rapidly discriminating the transmembrane β-barrels from other kinds of proteins. The model is fairly accurate, robust and can be run very efficiently on PC-like computers, thus proving useful for genome screening.
Type de document :
Article dans une revue
Methods in Molecular Biology -Clifton then Totowa-, Humana Press (Springer Imprint), 2013, 932, pp.277-94. 〈10.1007/978-1-62703-065-6_17〉
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https://hal.inria.fr/hal-00761759
Contributeur : Julie Bernauer <>
Soumis le : jeudi 6 décembre 2012 - 10:07:39
Dernière modification le : jeudi 11 janvier 2018 - 06:23:08

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Van Du T Tran, Philippe Chassignet, Jean-Marc Steyaert. Supersecondary structure prediction of transmembrane beta-barrel proteins.. Methods in Molecular Biology -Clifton then Totowa-, Humana Press (Springer Imprint), 2013, 932, pp.277-94. 〈10.1007/978-1-62703-065-6_17〉. 〈hal-00761759〉

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