Abstract
Accurate de novo design of transmembrane β-barrels would reduce the long standing dependency on hard-to-engineer natural protein ion channels with limited backbone geometries for nanopore-based single-molecule sensors. We have previously demonstrated that the de novo design of soluble eight-stranded β-barrels required considerable symmetry-breaking to achieve continuous hydrogen-bond connectivity and eliminate backbone strain. Here, using similar principles of backbone design we engineered eight-stranded transmembrane β-barrels with key turn sequences, mortise-tenon motifs and hydrophobic surface residues in silico with protein modeling software Rosetta, which is used to predict energy-optimized protein structures.
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