This would indicate an increased free energy of unfolding between the intermediate and the unfolded state.
Once sufficient unfolding occurs, the structure approaches a homogeneous, unfolded state (κ ≈ 0.12 Å-1).
Unfolding curves show a two-state folding mechanism, once unfolding occurs to the dimer it precedes to an unfolded state.
Thus, in addition to stabilising the unfolded state, force also reduces the free energy barrier to unfolding (or unbinding).
Of note, deep enthalpic traps at the unfolded state were observed on the folding landscape.
We find that the unfolded state has significant contributions from compact conformations.
Simulations in the presence of force lead to a highly extended unfolded state (see Fig. 4b).
This suggests that the intersection points contain overlapping FN dimers in an unfolded state.
The nature of the unfolded state plays a great role in our understanding of proteins.
The Effect of a ΔK280 Mutation on the Unfolded State of a Microtubule Binding Repeat in Tau.
Nonelectrostatic interactions, such as noncanonical interactions within the junctions and between junctions and helix stems, might further limit the conformational diversity of the unfolded state, resulting in a more ordered unfolded state than the one predicted from the electrostatic effect.
