López Bonilla, LuisCarpio Rodríguez, AnaPrados Montaño, Antonio2017-07-142017-07-142014-10López Bonilla, L., Carpio Rodríguez, A. y Prados Montaño, A. (2014). Protein unfolding and refolding as transitions through virtual states. Europhysics Letters, 108 (2), 28002-p1-28002-p6.0295-5075 (impreso)1286-4854 (electronico)http://hdl.handle.net/11441/62537Single-molecule atomic force spectroscopy probes elastic properties of titin, ubiquitin and other relevant proteins. We explain bioprotein folding dynamics under both length- and force-clamp by modeling polyprotein modules as particles in a bistable potential, weakly connected by harmonic spring linkers. Multistability of equilibrium extensions provides the characteristic sawtooth force-extension curve. We show that abrupt or stepwise unfolding and refolding under force-clamp conditions involve transitions through virtual states (which are quasi-stationary domain configurations) modified by thermal noise. These predictions agree with experimental observations.application/pdfengAttribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/Protein unfolding and refolding as transitions through virtual statesinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccesshttps://doi.org/10.1209/0295-5075/108/28002