2026-06-29T07:44:19Zhttps://docta.ucm.es/rest/oai/requestoai:docta.ucm.es:20.500.14352/338672024-07-09T16:12:24Zcom_20.500.14352_14col_20.500.14352_15
Protein unfolding and refolding as transitions through virtual states
Bonilla, Luis L.
Carpio Rodríguez, Ana María
Prados, Antonio
51
PACS 87.15.Cc –Folding: thermodynamics
Statistical mechanics
Models and pathways
PACS 05.40.-a – Fluctuation phenomena
Random processes
Noise and Brownian motion
PACS 87.14.et – Generic models (lattice
HP
Matemáticas (Matemáticas)
12 Matemáticas
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.
Ministerio de Economía, Comercio y Empresa (España)
Depto. de Análisis Matemático y Matemática Aplicada
Fac. de Ciencias Matemáticas
TRUE
pub
2023-06-19T13:29:46Z
2023-06-19T13:29:46Z
2014
journal article
https://hdl.handle.net/20.500.14352/33867
0295-5075
10.1209/0295-5075/108/28002
eng
FIS2011-28838- C02-01 (LLB)
FIS2011-28838-C02-02 (AC)
FIS2011- 24460 (AP)
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.
open access
application/pdf
EPL Association, European Physical Society