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Center for Nonlinear Studies |
This talk discusses our recent results using coarse-grained molecular dynamics protein folding models, which were previously optimized based on the energy landscape theory and the principle of minimal frustration, to gain insight into the folding of designed, simplified globular protein and α‐helical membrane proteins. Our work elucidates the role of topological versus energetic frustration in designed proteins and shows how they differ from those found for natural proteins; and how robust the folding of these designs would be to the simplification of the sequences using fewer amino acid types. With the addition of an implicit membrane energy term to the models, we are capable of predicting structures and binding interfaces of various membrane protein monomers and oligomers. More recent work allows us to characterize a near-native state of GlpG, an intramembrane protease, with potential functional significance that allows full-sized substrates to access the proteolytic site, and propose a solution to the major puzzle of negative phi values found in the experimental study of GlpG's folding mechanism.
Host: Angel E. Garcia