We discuss geometric and statistical models for analyzing spatial and sequence patterns in membrane proteins, as well as the possible roles of identified motifs in maintaining the structures and functions of membrane proteins. We further discuss how empirical potential functions can be developed to identify buried helices, to locate lipid-protein interfaces, and to find correct strand regisistration of membrane proteins. Finally, we describe preliminary results in ab initio prediction of atomic structures of beta-barrel membrane protein structures. (joint work with Larisa Adamian and Ronald Jackups, Jr. See www.uic.edu/~jliang for relevant publications).
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