The role of the turn in b-hairpin formation during WW domain folding

Sharpe, Tim and Jonsson, Amanda L. and Rutherford, Trevor J. and Daggett, Valerie and Fersht, Alan R.. (2007) The role of the turn in b-hairpin formation during WW domain folding. Protein Science, 1. pp. 2233-2239.

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Official URL: http://edoc.unibas.ch/47497/

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The folding of WW domains is rate limited by formation of a β-hairpin comprising residues from strands 1 and 2. Residues in the turn of this hairpin have reported Φ-values for folding close to 1 and have been proposed to nucleate folding. High Φ-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 β-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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > Biophysics Facility (Sharpe)
UniBasel Contributors:Sharpe, Timothy
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cambridge University Press
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:28 Nov 2017 08:12
Deposited On:28 Nov 2017 08:12

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