title: Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.
abstract: The Trp-cage, at 20 residues in length, is generally acknowledged as the smallest fully protein-like folding motif. Linking the termini by a two-residue unit and excising one residue affords circularly permuted sequences that adopt the same structure. This represents the first successful circular permutation of any fold of less than 50-residue length. As was observed for the original topology, a hydrophobic staple near the chain termini is required for enhanced fold stability.
authors.affiliation: Department of Chemistry, University of Washington Seattle, Washington, 98195, USA andersen@chem.washington.edu.
authors.forename: Aimee
authors.initials: A
authors.lastname: Byrne
authors.affiliation: Department of Chemistry, University of Washington Seattle, Washington, 98195, USA andersen@chem.washington.edu.
authors.forename: Brandon L
authors.initials: BL
authors.lastname: Kier
authors.affiliation: Department of Chemistry, University of Washington Seattle, Washington, 98195, USA andersen@chem.washington.edu.
authors.forename: D V
authors.initials: DV
authors.lastname: Williams
authors.affiliation: Department of Chemistry, University of Washington Seattle, Washington, 98195, USA andersen@chem.washington.edu.
authors.forename: Michele
authors.initials: M
authors.lastname: Scian
authors.affiliation: Department of Chemistry, University of Washington Seattle, Washington, 98195, USA andersen@chem.washington.edu.
authors.forename: Niels H
authors.initials: NH
authors.lastname: Andersen