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

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

2008-04-18

arxiv.org/abs/0804.2980v2

Europhys. Lett, 82, 58006 (2008)

Physics

Condensed Matter

Soft Condensed Matter

Scientific paper

10.1209/0295-5075/82/58006

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.

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