This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2m7d
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Trp-cage 16b P12W: a Hyperstable Miniprotein== | |
| - | + | <StructureSection load='2m7d' size='340' side='right' caption='[[2m7d]], [[NMR_Ensembles_of_Models | 30 NMR models]]' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M7D FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2m7c|2m7c]], [[2jof|2jof]], [[1l2y|1l2y]], [[1rij|1rij]], [[2ldj|2ldj]], [[2ll5|2ll5]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m7d RCSB], [http://www.ebi.ac.uk/pdbsum/2m7d PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24376912</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Andersen, N H | + | == References == |
| - | [[Category: Kier, B L | + | <references/> |
| - | [[Category: Williams, D V | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Andersen, N H]] | ||
| + | [[Category: Kier, B L]] | ||
| + | [[Category: Williams, D V]] | ||
[[Category: Circular permutant]] | [[Category: Circular permutant]] | ||
[[Category: De novo protein]] | [[Category: De novo protein]] | ||
Revision as of 17:55, 19 January 2015
Trp-cage 16b P12W: a Hyperstable Miniprotein
| |||||||||||
