Structural highlights
Publication Abstract from PubMed
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.
Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.,Byrne A, Kier BL, Williams DV, Scian M, Andersen NH RSC Adv. 2013 Nov 21;2013(43). doi: 10.1039/C3RA43674H. PMID:24376912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Byrne A, Kier BL, Williams DV, Scian M, Andersen NH. Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple. RSC Adv. 2013 Nov 21;2013(43). doi: 10.1039/C3RA43674H. PMID:24376912 doi:http://dx.doi.org/10.1039/C3RA43674H