Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2006 Jul 1;34(Web Server issue):W189-93.
doi: 10.1093/nar/gkl205.

transFold: a web server for predicting the structure and residue contacts of transmembrane beta-barrels

Affiliations

transFold: a web server for predicting the structure and residue contacts of transmembrane beta-barrels

J Waldispühl et al. Nucleic Acids Res. .

Abstract

Transmembrane beta-barrel (TMB) proteins are embedded in the outer membrane of Gram-negative bacteria, mitochondria and chloroplasts. The cellular location and functional diversity of beta-barrel outer membrane proteins makes them an important protein class. At the present time, very few non-homologous TMB structures have been determined by X-ray diffraction because of the experimental difficulty encountered in crystallizing transmembrane (TM) proteins. The transFold web server uses pairwise inter-strand residue statistical potentials derived from globular (non-outer-membrane) proteins to predict the supersecondary structure of TMB. Unlike all previous approaches, transFold does not use machine learning methods such as hidden Markov models or neural networks; instead, transFold employs multi-tape S-attribute grammars to describe all potential conformations, and then applies dynamic programming to determine the global minimum energy supersecondary structure. The transFold web server not only predicts secondary structure and TMB topology, but is the only method which additionally predicts the side-chain orientation of transmembrane beta-strand residues, inter-strand residue contacts and TM beta-strand inclination with respect to the membrane. The program transFold currently outperforms all other methods for accuracy of beta-barrel structure prediction. Available at http://bioinformatics.bc.edu/clotelab/transFold.

PubMed Disclaimer

Figures

Figure 1
Figure 1
(a) Linear representation of three consecutive and paired TM β-strands (standard output). Inter-strand residue contacts are indicated by arrows. (b) Sketch of a four-column tab-delimited text file summarizing the transFold prediction.
Figure 2
Figure 2
Input form for advanced users. The user can set bounds on the number of TM strands, bounds on strand length, shear number (inclination to plane), bounds on lengths of periplasmic and extra-cellular loops. In addition to choosing from a pull-down menu of a variety of hydrophobicity scales, the user can upload customized contact energies.

Similar articles

Cited by

References

    1. Gromiha M.M., Suwa M. A simple statistical method for discriminating outer membrane proteins with better accuracy. Bioinformatics. 2005;21:961–968. - PubMed
    1. Gromiha M.M., Ahmad S., Suwa M. TMBETA-NET: discrimination and prediction of membrane spanning beta-strands in outer membrane proteins. Nucleic Acids Res. 2005;33:W164–W167. - PMC - PubMed
    1. Bigelow H.R., Petrey D.S., Liu J., Przybylski D., Rost B. Predicting transmembrane beta-barrels in proteomes. Nucleic Acids Res. 2004;32:2566–2577. - PMC - PubMed
    1. Gromiha M.M., Ahmad S., Suwa M. Neural network-based prediction of transmembrane beta-strand segments in outer membrane proteins. J. Comput. Chem. 2004;25:762–767. - PubMed
    1. Natt N.K., Kaur H., Raghava G.P. Prediction of transmembrane regions of beta-barrel proteins using ANN- and SVM-based methods. Proteins. 2004;56:11–18. - PubMed

Publication types