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In a recent issue of PNAS, Libich et al. claim that apo-chaperonin GroEL has “intrinsic unfoldase/foldase activity” (1). However, the analysis of ref. 1 reveals that GroEL does not serve as a catalyst of folding/unfolding, because the claimed “20-fold” acceleration concerns only one step of the GroEL-involved transitions between the unfolded (I) and folded (F) forms of the studied protein (SH3Mut), whereas the GroEL-involved process as a whole is slower than the GroEL-free process. Thus, although transitions between the GroEL-bound states of SH3Mut (I-G↔F-G) are faster than I↔F transitions in the free protein, the I↔I-G step at the GroEL-involved pathway I↔I-G↔F-G↔F is slow, as it follows from the scheme presented by Libich et al. (1); it is reproduced in Fig. 1. A scheme of the protein folding/unfolding (1) with all kinetic constants k and the following from them relative concentrations (in percent) of …

Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps