Data from: Entropic bonding of the type 1 pilus from experiment and simulation

The type 1 pilus is a bacterial filament consisting of a long coiled
proteic chain of subunits joined together by non-covalent bonding between
complementing β-strands. Its strength and structural stability are
critical for its anchoring function in uropathogenic Escherichia
coli bacteria. The pulling and unravelling of the FimG subunit of
the pilus was recently studied by atomic force microscopy (AFM)
experiments and steered molecular dynamics (SMD) simulations [A.
Alonso-Caballero et al., Nature Commun. 9, 2758 (2018)]. In this work we
perform a quantitative comparison between experiment and simulation,
showing a good agreement in the underlying work values for the unfolding.
The simulation results are then used to estimate the free energy
difference for the detachment of FimG from the complementing strand of the
neighbouring subunit in the chain, FimF. Finally, we show that the large
free energy difference for the unravelling and detachment of the subunits
which leads to the high stability of the chain is entirely entropic in
nature.