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1l2y
From Proteopedia
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| - | [[ | + | ==NMR Structure of Trp-Cage Miniprotein Construct TC5b== |
| + | <StructureSection load='1l2y' size='340' side='right' caption='[[1l2y]], [[NMR_Ensembles_of_Models | 38 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1l2y]] is a 1 chain structure. The October 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Designer Proteins'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_10 10.2210/rcsb_pdb/mom_2005_10]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2Y FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jrj|1jrj]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l2y RCSB], [http://www.ebi.ac.uk/pdbsum/1l2y PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue constructs that are >95% folded in water at physiological pH. These constructs optimize a novel fold, designated as the 'Trp-cage' motif, and are significantly more stable than any other miniprotein reported to date. Folding is cooperative and hydrophobically driven by the encapsulation of a Trp side chain in a sheath of Pro rings. As the smallest protein-like construct, Trp-cage miniproteins should provide a testing ground for both experimental studies and computational simulations of protein folding and unfolding pathways. Pro Trp interactions may be a particularly effective strategy for the a priori design of self-folding peptides. | ||
| - | + | Designing a 20-residue protein.,Neidigh JW, Fesinmeyer RM, Andersen NH Nat Struct Biol. 2002 Jun;9(6):425-30. PMID:11979279<ref>PMID:11979279</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Designer Proteins]] | [[Category: Designer Proteins]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
Revision as of 14:00, 28 September 2014
NMR Structure of Trp-Cage Miniprotein Construct TC5b
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