2jof
From Proteopedia
(New page: 200px<br /><applet load="2jof" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jof" /> '''The Trp-cage: Optimizing the Stability of a ...) |
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| - | '''The Trp-cage: Optimizing the Stability of a Globular Miniprotein''' | + | {{Structure |
| + | |PDB= 2jof |SIZE=350|CAPTION= <scene name='initialview01'>2jof</scene> | ||
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| + | |GENE= | ||
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| + | '''The Trp-cage: Optimizing the Stability of a Globular Miniprotein''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JOF is a [ | + | 2JOF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOF OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Andersen, N H.]] | [[Category: Andersen, N H.]] | ||
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[[Category: two-state folding]] | [[Category: two-state folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:43:33 2008'' |
Revision as of 15:43, 20 March 2008
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The Trp-cage: Optimizing the Stability of a Globular Miniprotein
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).
About this Structure
2JOF is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 17:43:33 2008
