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.
The Trp-cage, at 20 residues in length, is generally acknowledged as the smallest fully n class="Chemical">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: Aimee Byrne; D Victoria Williams; Bipasha Barua; Stephen J Hagen; Brandon L Kier; Niels H Andersen Journal: Biochemistry Date: 2014-09-16 Impact factor: 3.162