  A theoretical analysis of the unfolding pathway of simple modular proteins in
length- controlled pulling experiments is put forward. Within this framework,
we predict the first module to unfold in a chain of identical units,
emphasizing the ranges of pulling speeds in which we expect our theory to hold.
These theoretical predictions are checked by means of steered molecular
dynamics of a simple construct, specifically a chain composed of two
coiled-coils motives, where anisotropic features are revealed. These
simulations also allow us to give an estimate for the range of pulling
velocities in which our theoretical approach is valid.
