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. 2004 Jul 1;32(Web Server issue):W400-4.
doi: 10.1093/nar/gkh417.

PRED-TMBB: a web server for predicting the topology of beta-barrel outer membrane proteins

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PRED-TMBB: a web server for predicting the topology of beta-barrel outer membrane proteins

Pantelis G Bagos et al. Nucleic Acids Res. .

Abstract

The beta-barrel outer membrane proteins constitute one of the two known structural classes of membrane proteins. Whereas there are several different web-based predictors for alpha-helical membrane proteins, currently there is no freely available prediction method for beta-barrel membrane proteins, at least with an acceptable level of accuracy. We present here a web server (PRED-TMBB, http://bioinformatics.biol.uoa.gr/PRED-TMBB) which is capable of predicting the transmembrane strands and the topology of beta-barrel outer membrane proteins of Gram-negative bacteria. The method is based on a Hidden Markov Model, trained according to the Conditional Maximum Likelihood criterion. The model was retrained and the training set now includes 16 non-homologous outer membrane proteins with structures known at atomic resolution. The user may submit one sequence at a time and has the option of choosing between three different decoding methods. The server reports the predicted topology of a given protein, a score indicating the probability of the protein being an outer membrane beta-barrel protein, posterior probabilities for the transmembrane strand prediction and a graphical representation of the assumed position of the transmembrane strands with respect to the lipid bilayer.

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Figures

Figure 1
Figure 1
Output of the prediction obtained from PRED-TMBB for the OmpX of E.coli. (A) The prediction of the transmembrane strands according to posterior decoding. (B) Plot of the posterior probabilities for the transmembrane strands, along the sequence. (C) Graphical representation of the predicted topology with respect to the lipid bilayer.

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