Abstract
A recent PNAS article (1) presents single-molecule fluorescence (SMF) data on the microsecond folding protein BBL, showing a bimodal FRET efficiency distribution near the denaturation midpoint, which is interpreted as direct evidence of two populations of molecules (folded and unfolded) separated by a free-energy barrier. This contrasts with our previous conclusion that BBL folds downhill (a single population that shifts during unfolding) based on quantitative analysis of a wealth of thermodynamic and kinetic data (see, for example, ref. 2). More surprisingly, we have independently performed SMF experiments on BBL and see a sharp unimodal distribution that shifts from high to low FRET efficiencies at increasing chemical denaturant (ref. 29 in ref. 1).
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