2jof
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1l2y|1l2y]], [[1jrj|1jrj]] | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/2jof PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jof RCSB]</span> | ||
}} | }} | ||
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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 Mon Mar 31 04:00:00 2008'' |
Revision as of 01:00, 31 March 2008
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| Related: | 1l2y, 1jrj
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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