Structural biology: analysis of `downhill` protein folding

Ferguson, Neil and Sharpe, Timothy D. and Johnson, Christopher M. and Schartau, Pamela J. and Fersht, Alan R.. (2007) Structural biology: analysis of `downhill` protein folding. Nature, 445 (7129). E14-E15.

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There is controversy as to whether homologues from the peripheral subunit binding domain family of small proteins fold `downhill` (that is, non-cooperatively, in the absence of free-energy barriers between conformations) and whether they modulate their size for biological function. Sadqi et al. claim that Naf-BBL-a naphthylalanine-labelled, truncated version of this domain-folds in this way, on the grounds that they recorded a wide spread of melting temperatures of individual atoms measured by proton nuclear magnetic resonance (NMR) during their thermal denaturation. But their data are not of adequate quality to distinguish, within experimental error, between downhill folding and folding with a cooperative transition. Accordingly, their results offer no compelling evidence that Naf-BBL folds downhill, particularly as non-truncated, unmodified peripheral subunit binding domains seem to fold cooperatively.
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
Note:Publication type according to Uni Basel Research Database: Journal article -- Discussion on page E17
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Last Modified:28 Nov 2017 08:19
Deposited On:28 Nov 2017 08:18

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