2m7d
From Proteopedia
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| - | {{STRUCTURE_2m7d| PDB=2m7d | SCENE= }} | ||
| - | ===Trp-cage 16b P12W: a Hyperstable Miniprotein=== | ||
| - | == | + | ==Trp-cage 16b P12W: a Hyperstable Miniprotein== |
| - | [[2m7d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M7D OCA]. | + | <StructureSection load='2m7d' size='340' side='right'caption='[[2m7d]]' scene=''> |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2m7d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M7D FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m7d OCA], [https://pdbe.org/2m7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m7d RCSB], [https://www.ebi.ac.uk/pdbsum/2m7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m7d ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | <div style="background-color:#fffaf0;"> |
| - | [[Category: | + | == 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. | ||
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| + | 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<ref>PMID:24376912</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2m7d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Andersen NH]] | ||
| + | [[Category: Kier BL]] | ||
| + | [[Category: Williams DV]] | ||
Current revision
Trp-cage 16b P12W: a Hyperstable Miniprotein
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