2m7c | pdb_00002m7c

Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple

spinqualitylabelsall models 2m7c Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m7c is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AIB, DAL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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