Carpio Rodríguez, Ana María2023-06-172023-06-172019-05https://hdl.handle.net/20.500.14352/14204Single-molecule atomic force spectroscopy probes elastic properties of proteins such as titin and ubiquitin. We analyze bioprotein folding dynamics under both force and length-clamp conditions by modeling polyprotein modules as particles in a bistable potential, connected by harmonic springs. The study of multistable equilibria in these models explains recorded sawtooth force-extension curves. We show that bifurcations and transitions through quasi-stationary domain configurations modified by thermal noise are involved in observed stepwise and abrupt refolding and unfolding phenomena under force-clamp conditions. These predictions agree with experimental observations.engconference paperopen accessBiomatemáticas2404 Biomatemáticas