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The mechanical unfolding of an engineered protein composed of eight domainsof Ig27 is investigated by using atomic force microscopy. Exploiting afluctuation relation, the equilibrium free energy as a function of the moleculeelongation is estimated from pulling experiments. Such a free energy exhibits aregular shape that sets a typical unfolding length at zero force of the orderof 20 nm. This length scale turns out to be much larger than the kineticunfolding length that is also estimated by analyzing the typical rupture forceof the molecule under dynamic loading.

Reconstructing the free energy landscape of a polyprotein by single-molecule experiments