Abstract
The force-dependent unfolding/refolding of protein domains and ligand-receptor association/dissociation are crucial for mechanosensitive functions, while many aspects of how force affects the transition rate still remain poorly understood. Here, we report a new analytical expression of the force-dependent rate of molecules for 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 are not restricted by the shape and dimensionality of the underlying free energy landscape. Importantly, the parameters of this model provide direct information on the structural-elastic features of the molecules between their transition and initial states. We demonstrate the applications of this model by applying it to explain force-dependent transition kinetics for several molecules and predict the structural-elastic properties of the transition states of these molecules.