Supersecondary structure prediction of transmembrane beta-barrel proteins.

Van Du T Tran 1 Philippe Chassignet 1 Jean-Marc Steyaert 1, 2
2 AMIB - Algorithms and Models for Integrative Biology
LIX - Laboratoire d'informatique de l'École polytechnique [Palaiseau], LRI - Laboratoire de Recherche en Informatique, UP11 - Université Paris-Sud - Paris 11, Inria Saclay - Ile de France
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.
Document type :
Journal articles
Complete list of metadatas

https://hal.inria.fr/hal-00761759
Contributor : Julie Bernauer <>
Submitted on : Thursday, December 6, 2012 - 10:07:39 AM
Last modification on : Wednesday, March 27, 2019 - 4:41:29 PM

Identifiers

Collections

Citation

Van Du T Tran, Philippe Chassignet, Jean-Marc Steyaert. Supersecondary structure prediction of transmembrane beta-barrel proteins.. Methods in Molecular Biology, Humana Press/Springer Imprint, 2013, Protein Supersecondary Structures, 932, pp.277-294. ⟨10.1007/978-1-62703-065-6_17⟩. ⟨hal-00761759⟩

Share

Metrics

Record views

425