Protein unfolding and refolding as transitions through virtual states
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2014
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EPL Association, European Physical Society
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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.
Abstract
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.