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EMBO reports 6, 1, 46–51 (2005)
doi:10.1038/sj.embor.7400317
Published online: 17 December 2004
Figure 4
The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments
Ingo Schwaiger, Michael Schleicher, Angelika A Noegel & Matthias Rief
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Single-molecule folding and unfolding kinetics of ddFLN4. (A) Fraction of observed events for mechanical refolding as a function of the allowed refolding time (red: no refolding; green: complete refolding; blue: refolding to RFI). For each time point at 5, 10, 20, 30 and 40 ms, 1,377, 404, 417, 536 and 270 events were analysed, respectively. The lines are fits according to the kinetic folding scheme shown at the top with k1=55 4 s-1 and k2=17920 s-1 (see Methods). (B) Histograms of unfolding forces for unfolding from native state N to UFI (left), from RFI to unfolded state U (middle) and from UFI to U (right). The solid lines in the left and middle histograms are fits according to a two-state model (see text and Methods).
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