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[[Image:2jof.png|left|200px]]
==The Trp-cage: Optimizing the Stability of a Globular Miniprotein==
<StructureSection load='2jof' size='340' side='right' caption='[[2jof]], [[NMR_Ensembles_of_Models | 28 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jof]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JOF FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l2y|1l2y]], [[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=2jof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jof RCSB], [http://www.ebi.ac.uk/pdbsum/2jof PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Trp-cage, as the smallest miniprotein, remains the subject of numerous computational and experimental studies of protein folding dynamics and pathways. The original Trp-cage (NLYIQWLKDGGPSSGRPPPS, Tm = 42 degrees C) can be significantly stabilized by mutations; melting points as high as 64 degrees C are reported. In helical portions of the structure, each allowed replacement of Leu, Ile, Lys or Ser residues by Ala results in a 1.5 (+/-0.35) kJ/mol fold stabilization. No changes in structure or fluxionality of the core results upon stabilization. Contrary to the initial hypothesis, specific Pro/Trp interactions are not essential for core formation. The entropic advantage of Pro versus Ala (DeltaDeltaS(U) = 11 +/- 2 J/mol K) was measured at the solvent-exposed P17 site. Pro-Ala mutations at two of the three prolines (P12 and P18) that encage the indole ring result in less fold destabilization (2.3-3.4 kJ/mol). However, a P19A mutation reduces fold stability by 16 kJ/mol reflecting a favorable Y3/P19 interaction as well as Trp burial. The Y3/P19 hydrophobic staple interaction defines the folding motif as an 18-residue unit. Other stabilizing features that have been identified include a solvent-exposed Arg/Asp salt bridge (3.4-6 kJ/mol) and a buried H-bonded Ser side chain ( approximately 10 kJ/mol).


{{STRUCTURE_2jof|  PDB=2jof  |  SCENE=  }}
The Trp-cage: optimizing the stability of a globular miniprotein.,Barua B, Lin JC, Williams VD, Kummler P, Neidigh JW, Andersen NH Protein Eng Des Sel. 2008 Mar;21(3):171-85. Epub 2008 Jan 18. PMID:18203802<ref>PMID:18203802</ref>


===The Trp-cage: Optimizing the Stability of a Globular Miniprotein===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_18203802}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2jof]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOF OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:018203802</ref><references group="xtra"/>
[[Category: Andersen, N H.]]
[[Category: Andersen, N H.]]
[[Category: Barua, B.]]
[[Category: Barua, B.]]
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