2M7D
Trp-cage 16b P12W: a Hyperstable Miniprotein
Summary for 2M7D
| Entry DOI | 10.2210/pdb2m7d/pdb |
| Related | 1l2y 1rij 2jof 2ldj 2ll5 2m7c |
| NMR Information | BMRB: 19183 |
| Descriptor | Trp-Cage mini-protein (1 entity in total) |
| Functional Keywords | miniprotein, de novo protein, trp-cage, circular permutant, microprotein |
| Total number of polymer chains | 1 |
| Total formula weight | 2131.28 |
| Authors | Williams, D.V.,Andersen, N.H.,Kier, B.L. (deposition date: 2013-04-19, release date: 2013-12-25, Last modification date: 2024-11-06) |
| Primary citation | Byrne, A.,Kier, B.L.,Williams, D.V.,Scian, M.,Andersen, N.H. Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple. RSC Adv, 2013:19824-19829, 2013 Cited by PubMed 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. PubMed: 24376912DOI: 10.1039/C3RA43674H PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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