RT Journal Article
T1 Protein unfolding and refolding as transitions through virtual states
A1 Bonilla, Luis L.
A1 Carpio Rodríguez, Ana María
A1 Prados, Antonio
AB 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.
PB EPL Association, European Physical Society
SN 0295-5075
YR 2014
FD 2014
LK https://hdl.handle.net/20.500.14352/33867
UL https://hdl.handle.net/20.500.14352/33867
LA eng
NO 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.
NO Ministerio de Economía, Comercio y Empresa (España)
DS Docta Complutense
RD 13 may 2025