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1l2y

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(New page: 200px<br /> <applet load="1l2y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2y" /> '''NMR Structure of Trp-Cage Miniprotein Const...)
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[[Image:1l2y.gif|left|200px]]<br />
 
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<applet load="1l2y" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l2y" />
 
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'''NMR Structure of Trp-Cage Miniprotein Construct TC5b'''<br />
 
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==Overview==
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==NMR Structure of Trp-Cage Miniprotein Construct TC5b==
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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.
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<StructureSection load='1l2y' size='340' side='right'caption='[[1l2y]]' scene=''>
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== Structural highlights ==
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1L2Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L2Y OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Designing a 20-residue protein., Neidigh JW, Fesinmeyer RM, Andersen NH, Nat Struct Biol. 2002 Jun;9(6):425-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11979279 11979279]
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</div>
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<div class="pdbe-citations 1l2y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Designer Proteins]]
[[Category: Designer Proteins]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Andersen, N.H.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Fesinmeyer, R.M.]]
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[[Category: Andersen NH]]
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[[Category: Neidigh, J.W.]]
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[[Category: Fesinmeyer RM]]
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[[Category: miniprotein]]
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[[Category: Neidigh JW]]
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[[Category: trp-cage]]
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[[Category: two-state folding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:03:11 2007''
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Current revision

NMR Structure of Trp-Cage Miniprotein Construct TC5b

PDB ID 1l2y

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