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One-state downhill versus conventional protein folding

Ferguson, Neil and Schartau, Pamela J. and Sharpe, Timothy D. and Sato, Satoshi and Fersht, Alan R.. (2004) One-state downhill versus conventional protein folding. Journal of Molecular Biology, 344 (2). pp. 295-301.

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Official URL: http://edoc.unibas.ch/47503/

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Abstract

Classical protein folding invokes a cooperative transition between distinct thermodynamic states that are individually populated at equilibrium and separated by an energy barrier. It has been proposed, however, that the small protein, BBL, undergoes one-step downhill folding whereby it folds non-cooperatively to its native state without encountering an appreciable energy barrier. Only a single conformational ensemble is populated under given conditions, and so the denatured state ensemble progressively changes into the native structure. A wide dispersion of thermal denaturation midpoints that was observed for an extrinsically labelled fragment of BBL is proposed to be evidence for its one-state, downhill folding, a phenomenon that is also suggested to be functionally important for BBL and its homologues. We found, however, that thermal denaturation of unlabelled wild-type BBL was highly cooperative, with very similar transition midpoints for the melting of secondary and tertiary interactions, as well as for individual residues when monitored by NMR. Similar results were also observed for two other homologues, E3BD and POB. Further, the extrinsic fluorophores perturbed the unfolding energetics of labelled BBL, and complicated its equilibrium behaviour. One-step downhill folding may well occur for some proteins that do not have distinct folded states but not for BBL and its well-folded homologues.
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:Elsevier
ISSN:0022-2836
e-ISSN:1089-8638
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:27 Nov 2017 08:02
Deposited On:27 Nov 2017 08:02

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