1l2y: Difference between revisions

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[[Image:1l2y.png|left|200px]]


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==NMR Structure of Trp-Cage Miniprotein Construct TC5b==
The line below this paragraph, containing "STRUCTURE_1l2y", creates the "Structure Box" on the page.
<StructureSection load='1l2y' size='340' side='right'caption='[[1l2y]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_1l2y|  PDB=1l2y  |  SCENE=  }}
</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 &gt;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.


'''NMR Structure of Trp-Cage Miniprotein Construct TC5b'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
{{ABSTRACT_11979279}}
</div>
 
<div class="pdbe-citations 1l2y" style="background-color:#fffaf0;"></div>
==About this Structure==
== References ==
The following page contains interesting information on the relation of 1L2Y with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2Y OCA].
<references/>
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</StructureSection>
[[Category: Designer Proteins]]
[[Category: Designer Proteins]]
[[Category: Andersen, N H.]]
[[Category: Large Structures]]
[[Category: Fesinmeyer, R M.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Neidigh, J W.]]
[[Category: Andersen NH]]
[[Category: Miniprotein]]
[[Category: Fesinmeyer RM]]
[[Category: Trp-cage]]
[[Category: Neidigh JW]]
[[Category: Two-state folding]]
 
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