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oai:docta.ucm.es:20.500.14352/338672024-07-09T16:12:24Zcom_20.500.14352_14col_20.500.14352_15

00925njm 22002777a 4500 dc Bonilla, Luis L. author Carpio Rodríguez, Ana María author Prados, Antonio author 2014 Single-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. Bonilla, L. L., Carpio Rodríguez, A. M., Prados, A. «Protein unfolding and refolding as transitions through virtual states». EPL (Europhysics Letters), vol. 108, n.o 2, octubre de 2014, p. 28002. DOI.org (Crossref), https://doi.org/10.1209/0295-5075/108/28002. 0295-5075 10.1209/0295-5075/108/28002 https://hdl.handle.net/20.500.14352/33867 https://doi.org/10.1209/0295-5075/108/28002 http://iopscience.iop.org/0295-5075/108/2/28002 Protein unfolding and refolding as transitions through virtual states