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[[Image:2jof.jpg|left|200px]]


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==The Trp-cage: Optimizing the Stability of a Globular Miniprotein==
The line below this paragraph, containing "STRUCTURE_2jof", creates the "Structure Box" on the page.
<StructureSection load='2jof' size='340' side='right'caption='[[2jof]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2jof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2JOF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=2jof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jof OCA], [https://pdbe.org/2jof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jof RCSB], [https://www.ebi.ac.uk/pdbsum/2jof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jof ProSAT]</span></td></tr>
{{STRUCTURE_2jof| PDB=2jof  |  SCENE= }}
</table>
 
<div style="background-color:#fffaf0;">
'''The Trp-cage: Optimizing the Stability of a Globular Miniprotein'''
== Publication Abstract from PubMed ==
 
 
==Overview==
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).
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).


==About this Structure==
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>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOF OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/18203802 18203802]
</div>
[[Category: Andersen, N H.]]
<div class="pdbe-citations 2jof" style="background-color:#fffaf0;"></div>
[[Category: Barua, B.]]
== References ==
[[Category: De novo protein]]
<references/>
[[Category: Miniprotein]]
__TOC__
[[Category: Trp-cage]]
</StructureSection>
[[Category: Two-state folding]]
[[Category: Large Structures]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:06:37 2008''
[[Category: Synthetic construct]]
[[Category: Andersen NH]]
[[Category: Barua B]]

Latest revision as of 10:09, 20 December 2023

The Trp-cage: Optimizing the Stability of a Globular Miniprotein

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