2jof
From Proteopedia
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[[Image:2jof.jpg|left|200px]] | [[Image:2jof.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_2jof| PDB=2jof | SCENE= }} | |
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'''The Trp-cage: Optimizing the Stability of a Globular Miniprotein''' | '''The Trp-cage: Optimizing the Stability of a Globular Miniprotein''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | 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://www.ncbi.nlm.nih.gov/pubmed/18203802 18203802] | 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: Andersen, N H.]] | [[Category: Andersen, N H.]] | ||
[[Category: Barua, B.]] | [[Category: Barua, B.]] | ||
| - | [[Category: | + | [[Category: De novo protein]] |
| - | [[Category: | + | [[Category: Miniprotein]] |
| - | [[Category: | + | [[Category: Trp-cage]] |
| - | [[Category: | + | [[Category: Two-state folding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:06:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:06, 4 May 2008
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
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 Sun May 4 09:06:37 2008
