WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state.

  • Koepf E
  • Petrassi H
  • Sudol M
 et al. 
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The objective of this study was to evaluate the suitability of the WW domain as a desirable model system to understand the folding and stability of an isolated three-stranded antiparallel beta-sheet structure. The WW domain was subjected to thermal and chaotropic denaturation/reconstitution utilizing a variety of biophysical methods. This three-stranded sheet folds reversibly and cooperatively utilizing both urea and GdnHCl as denaturants; however, the denatured state retains structure in the form of a hydrophobic cluster involving at least one aromatic side chain. In contrast to chaotropic denaturation, thermal denaturation appears to be more complete and may be a two state process. The suitability of the WW domain for future studies aimed at understanding the kinetics and thermodynamics of antiparallel beta-sheet folding clearly emerges from this initial study. The most exciting and significant result in this manuscript is the finding that the chaotropic denatured state of WW has a hydrophobic cluster as discerned by near-UV CD evidence. The role that the denatured state plays in the folding and stability of a three-stranded beta-sheets, and its capacity for preventing aggregation may be particularly important and is the subject of ongoing studies.

Author-supplied keywords

  • a recently discovered protein
  • antiparallel b -sheet structure
  • b -sheet folding
  • conserved trp residues separated
  • for the two highly
  • hydrophobic cluster
  • in the se-
  • ing of a three-stranded
  • module consist-
  • reversible folding
  • that is named
  • the ww domain is
  • ww

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  • E K Koepf

  • H M Petrassi

  • M Sudol

  • J W Kelly

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