The role of the turn in β-hairpin formation during WW domain folding
| Autor: | Valerie Daggett, Alan R. Fersht, Timothy Sharpe, Trevor J. Rutherford, Amanda L. Jonsson |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Protein Folding biology Chemistry Hydrogen Bonding Phi value analysis Contact order Biochemistry Protein Structure Secondary Article Protein Structure Tertiary WW domain Folding (chemistry) Turn (biochemistry) Molecular dynamics Crystallography medicine.anatomical_structure biology.protein medicine Downhill folding Nuclear Magnetic Resonance Biomolecular Molecular Biology Nucleus |
| Zdroj: | Protein Science. 16:2233-2239 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1110/ps.073004907 |
| Popis: | The folding of WW domains is rate limited by formation of a beta-hairpin comprising residues from strands 1 and 2. Residues in the turn of this hairpin have reported Phi-values for folding close to 1 and have been proposed to nucleate folding. High Phi-values do not necessarily imply that the energetics of formation are a driving force for initiating folding. We demonstrate by NMR studies and molecular dynamics simulations that the first turn of the hYAP, FBP28, and PIN1 WW domains is structurally dynamic and solvent exposed in the native and folding transition states. It is, therefore, unlikely that the formation of the beta-turn per se provides the energetic driving force for hairpin folding. It is more likely that the turn acts as an easily formed hinge that facilitates the formation of the hairpin; it is a nucleus as defined by the nucleation-condensation mechanism whereby a diffuse nucleus is stabilized by associated interactions. |
| Databáze: | OpenAIRE |
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