The mechanical unfolding of an engineered protein composed of eight domains of Ig27 is investigated by using atomic force microscopy. Exploiting a fluctuation relation, the equilibrium free energy as a function of the molecule elongation is estimated from pulling experiments. Such a free energy exhibits a regular shape that sets a typical unfolding length at zero force of the order of 20 nm. This length scale turns out to be much larger than the kinetic-unfolding length that is also estimated by analyzing the typical rupture force of the molecule under dynamic loading.
Reconstructing the free-energy landscape of a polyprotein by single-molecule experiments
F Sbrana;M Vassalli
2008
Abstract
The mechanical unfolding of an engineered protein composed of eight domains of Ig27 is investigated by using atomic force microscopy. Exploiting a fluctuation relation, the equilibrium free energy as a function of the molecule elongation is estimated from pulling experiments. Such a free energy exhibits a regular shape that sets a typical unfolding length at zero force of the order of 20 nm. This length scale turns out to be much larger than the kinetic-unfolding length that is also estimated by analyzing the typical rupture force of the molecule under dynamic loading.File in questo prodotto:
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