Beta-barrel membrane proteins are found in the outer membrane of gram-negative bacteria, mitochondria, and chloroplasts. They are important for pore formation, membrane anchoring, enzyme activity, and are often responsible for bacterial virulence. Due to difficulties in experimental structure determination, they are sparsely represented in the protein structure databank. We have developed a webserver (TMBB-Explorer) capable of predicting the three-dimensional structure, oligomerization state, protein-protein interaction interface, and thermodynamic properties such as heat capacity and relative melting temperature of the transmembrane domains of beta-barrel membrane proteins. Our method is based on a physical interaction model, a simplified conformational space for efficient enumeration, and an empirical potential function from a detailed combinatorial analysis [1]. It also accounts for loop entropy and an affinity for right-handedness of the natural beta-barrels. The webserver also reports the hydrogen bonds formed between the beta-strands in the predicted structure. The webserver can provide predictions using sequence information alone or by incorporating secondary structure information.[1] Naveed et al. Proc. Natl. Acad. Sci. USA, 106(31):12735-12740.