Analysis of 'downhill' protein folding

Neil Ferguson (), Timothy D. Sharpe (), Christopher M. Johnson (), Pamela J. Schartau () and Alan R. Fersht ()
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Neil Ferguson: Medical Research Council Centre for Protein Engineering, Medical Research Council Centre
Timothy D. Sharpe: Medical Research Council Centre for Protein Engineering, Medical Research Council Centre
Christopher M. Johnson: Medical Research Council Centre for Protein Engineering, Medical Research Council Centre
Pamela J. Schartau: Medical Research Council Centre for Protein Engineering, Medical Research Council Centre
Alan R. Fersht: Medical Research Council Centre for Protein Engineering, Medical Research Council Centre

Nature, 2007, vol. 445, issue 7129, E14-E15

Abstract: Abstract Arising from: M. Sadqi, D. Fushman & V. Muñoz Nature 442, 317–321 (2006)10.1038/nature04859 ; M. Sadqi et al. reply 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.1 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 cooperatively2,3.

Date: 2007
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DOI: 10.1038/nature05643

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