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PRED-TMBB: a web server for predicting the topology of -barrel outer membrane proteins
Author(s) -
Pantelis G. Bagos,
TH. D. LIAKOPOULOS,
Ioannis C Spyropoulos,
Stavros J. Hamodrakas
Publication year - 2004
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkh417
Subject(s) - transmembrane protein , bacterial outer membrane , biology , membrane protein , barrel (horology) , membrane topology , porin , transmembrane domain , computational biology , topology (electrical circuits) , membrane , biochemistry , mathematics , gene , materials science , combinatorics , receptor , escherichia coli , composite material
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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