  The lifetime of protein domains and ligand-receptor complexes under force is
crucial for mechanosensitive functions, while many aspects of how force affects
the lifetime still remain poorly understood. Here, we report a new analytical
expression of the force-dependent molecular lifetime to understand transitions
overcoming a single barrier. Unlike previous models derived in the framework of
Kramers theory that requires a presumed one-dimensional free energy landscape,
our model is derived based on the structural-elastic properties of molecules
which is not restricted by the shape and dimensionality of the underlying free
energy landscape. Importantly, the parameters of this model provide direct
information of the structural-elastic features of the molecules between the
transition and the native states. We demonstrate the applications of this model
by applying it to explain complex force-dependent lifetime data for several
molecules reported in recent experiments, and predict the structural-elastic
properties of the transition states of these molecules.
