Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.
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ABSTRACT:
SUBMITTER: Byrne A
PROVIDER: S-EPMC3870897 | biostudies-literature | 2013 Nov
REPOSITORIES: biostudies-literature
Publications
Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.
Byrne Aimee A Kier Brandon L BL Williams D V DV Scian Michele M Andersen Niels H NH
RSC advances 20131101 43
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. ...[more]
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