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The lifetime of protein domains and ligand-receptor complexes under force iscrucial for mechanosensitive functions, while many aspects of how force affectsthe lifetime still remain poorly understood. Here, we report a new analyticalexpression of the force-dependent molecular lifetime to understand transitionsovercoming a single barrier. Unlike previous models derived in the framework ofKramers theory that requires a presumed one-dimensional free energy landscape,our model is derived based on the structural-elastic properties of moleculeswhich is not restricted by the shape and dimensionality of the underlying freeenergy landscape. Importantly, the parameters of this model provide directinformation of the structural-elastic features of the molecules between thetransition and the native states. We demonstrate the applications of this modelby applying it to explain complex force-dependent lifetime data for severalmolecules reported in recent experiments, and predict the structural-elasticproperties of the transition states of these molecules.

Structural-elastic determination of the mechanical lifetime of biomolecules