Abstract
β-barrel membrane proteins (βMPs), found in the outer membrane of gram-negative bacteria, mitochondria, and chloroplasts, play important roles in membrane anchoring, pore formation, and enzyme activities. However, it is often difficult to determine their structures experimentally, and the knowledge of their structures is currently limited. We have developed a method to predict the 3D architectures of βMPs. We can accurately construct transmembrane domains of βMPs by predicting their strand registers, from which full 3D atomic structures are derived. Using 3D Beta-barrel Membrane Protein Predictor (3D-BMPP), we can further accurately model the extended beta barrels and loops in non-TM regions with overall greater structure prediction coverage. 3DBMPP is a general technique that can be applied to protein families with limited sequences as well as proteins with novel folds. Applications of 3DBMPP can be broadly applied to genome-wide βMPs structure prediction.
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