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
| Autor: | Edward K. Koepf, Jeffery W. Kelly, H M Petrassi, Marius Sudol |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Protein Denaturation
Protein Folding Magnetic Resonance Spectroscopy Biochemical Phenomena Beta sheet Antiparallel (biochemistry) Biochemistry Protein Structure Secondary WW domain chemistry.chemical_compound Protein structure Humans Urea Denaturation (biochemistry) Guanidine Molecular Biology Adaptor Proteins Signal Transducing Models Statistical biology Dose-Response Relationship Drug Circular Dichroism Temperature YAP-Signaling Proteins Phosphoproteins Protein Structure Tertiary Chaotropic agent Crystallography Kinetics Spectrometry Fluorescence chemistry biology.protein Thermodynamics Protein folding Carrier Proteins Protein Binding Transcription Factors Research Article |
| Zdroj: | Protein science : a publication of the Protein Society. 8(4) |
| ISSN: | 0961-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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