  Mechanically induced unfolding of passive crosslinkers is a fundamental
biological phenomenon encountered across the scales from individual
macro-molecules to cytoskeletal actin networks. In this paper we study a
conceptual model of athermal load-induced unfolding and use a minimalistic
setting allowing one to emphasize the role of long-range interactions while
maintaining full analytical transparency. Our model can be viewed as a
description of a parallel bundle of N bistable units confined between two
shared rigid backbones that are loaded through a series spring. We show that
the ground states in this model correspond to synchronized, single phase
configurations where all individual units are either folded or unfolded. We
then study the fine structure of the wiggly energy landscape along the reaction
coordinate linking the two coherent states and describing the optimal mechanism
of cooperative unfolding. Quite remarkably, our study shows the fundamental
difference in the size and structure of the folding-unfolding energy barriers
in the hard (fixed displacements) and soft (fixed forces) loading devices which
persists in the continuum limit. We argue that both, the synchronization and
the non-equivalence of the mechanical responses in hard and soft devices, have
their origin in the dominance of long-range interactions. We then apply our
minimal model to skeletal muscles where the power-stroke in acto-myosin
crossbridges can be interpreted as passive folding. A quantitative analysis of
the muscle model shows that the relative rigidity of myosin backbone provides
the long-range interaction mechanism allowing the system to effectively
synchronize the power-stroke in individual crossbridges even in the presence of
thermal fluctuations. In view of the prototypical nature of the proposed model,
our general conclusions pertain to a variety of other biological systems where
elastic interactions are mediated by effective backbones.
