1l2y: Difference between revisions
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==NMR Structure of Trp-Cage Miniprotein Construct TC5b== | |||
<StructureSection load='1l2y' size='340' side='right'caption='[[1l2y]]' scene=''> | |||
== Structural highlights == | |||
| | <table><tr><td colspan='2'>[[1l2y]] is a 1 chain structure. The October 2005 RCSB PDB [https://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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1L2Y FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2y OCA], [https://pdbe.org/1l2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2y RCSB], [https://www.ebi.ac.uk/pdbsum/1l2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2y ProSAT]</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. | 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> | |||
<div class="pdbe-citations 1l2y" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Designer Proteins]] | [[Category: Designer Proteins]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: | [[Category: Andersen NH]] | ||
[[Category: | [[Category: Fesinmeyer RM]] | ||
[[Category: | [[Category: Neidigh JW]] | ||
