2m7d: Difference between revisions

Line 1:

~~{{STRUCTURE_2m7d~~| ~~PDB~~=2m7d | ~~SCENE~~= }}

==Trp-cage 16b P12W: a Hyperstable Miniprotein==

===~~Trp~~-~~cage 16b P12W~~: ~~a Hyperstable Miniprotein~~===

~~{{ABSTRACT_PUBMED_24376912}}~~

== 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='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>

== 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.

~~==About this Structure==~~

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>

~~[[2m7d]] is~~ a ~~1 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.ac.il/~~oca-bin~~/~~ocashort?id=2M7D OCA].~~

==~~Reference~~==

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~<ref group="xtra">PMID:024376912</ref>~~<references ~~group="xtra"~~/><~~references~~/>

</div>

[[Category: Andersen, N H.]]

== References ==

[[Category: Kier, B L.]]

[[Category: Williams, D V.]]

__TOC__

</StructureSection>

[[Category: Andersen, N H]]

[[Category: Kier, B L]]

[[Category: Williams, D V]]

[[Category: Circular permutant]]

[[Category: De novo protein]]

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_2m7d|  PDB=2m7d  |  SCENE=  }}
+==Trp-cage 16b P12W: a Hyperstable Miniprotein==
-===Trp-cage 16b P12W: a Hyperstable Miniprotein===
+<StructureSection load='2m7d' size='340' side='right' caption='[[2m7d]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
-{{ABSTRACT_PUBMED_24376912}}
+== 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.
-==About this Structure==
+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>
-[[2m7d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M7D OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:024376912</ref><references group="xtra"/><references/>
+</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: De novo protein]]