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My research group is focused on using molecular simulation methods, in close collaboration with experimentalists, to predict and design the conformation, dynamics, and binding of proteins and peptidomimetics. At Temple, I have been working towards a new challenge: the design of foldable peptidomimetics. I have extensive expertise using large-scale simulation to understand protein folding, and an excellent track record of collaboration with experimentalists to study conformational dynamics of proteins (JACS 2010, 2012). The most recent example of this is an ongoing collaboration with Heinrich Roder on an NSF-funded project to elucidate early folding events in apomyoglobin. In another example, I headed a team of top research groups studying foldable peptide mimics called peptoids (oligomers of N-substituted glycine), to publish the first example of blind structure prediction of a cyclic peptoid nonamer (PNAS 2012). Our focus on foldable peptidomimetics has forged strong collaborations within our department, as well as Fox Chase Cancer Center's Molecular Therapeutics Program. We are involved in several ongoing collaborations in this area: one with Bill Wuest at Temple to computational model and design foldable cyclic peptide beta-hairpin mimics to inhibit the LapD-LapG interface important in biofilm formation (JCIM 2014). The other is with Christian Schafmeister at Temple to predict and design functional spiroligomer bundles for binding and catalysis. Our most recent published work has focused on modeling conformational pre-organization of cyclic RGD peptides (small beta-turn mimic inhibitors of integrin, JCIM 2015) and new computational methods for combining simulations and experiment to infer conformational populations of peptidomimetic ligands in solution (BICePs, JCC 2014).