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Updated: Aug 4, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Prediction of beta-barrel membrane proteins by searching for restricted domains
Oliver Mirus1, Enrico Schleiff
1Botanisches Institut der Ludwig-Maximilians-Universität München, Menzinger Str. 67, 80638 München, Germany. mirus@lrz.uni-muenchen.de
Background:
The identification of beta-barrel membrane proteins out of a genomic/proteomic background is one of the rapidly developing fields in bioinformatics. Our main goal is the prediction of such proteins in genome/proteome wide analyses.
Results:
For the prediction of beta-barrel membrane proteins within prokaryotic proteomes a set of parameters was developed. We have focused on a procedure with a low false positive rate beside a procedure with lowest false prediction rate to obtain a high certainty for the predicted sequences. We demonstrate that the discrimination between beta-barrel membrane proteins and other proteins is improved by analyzing a length limited region. The developed set of parameters is applied to the proteome of E. coli and the results are compared to four other described procedures.
Conclusion:
Analyzing the beta-barrel membrane proteins revealed the presence of a defined membrane inserted beta-barrel region. This information can now be used to refine other prediction programs as well. So far, all tested programs fail to predict outer membrane proteins in the proteome of the prokaryote E. coli with high reliability. However, the reliability of the prediction is improved significantly by a combinatory approach of several programs. The consequences and usability of the developed scores are discussed.
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