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Protein unfolding and refolding as transitions through virtual states

 

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Author: López Bonilla, Luis
Carpio Rodríguez, Ana
Prados Montaño, Antonio
Department: Universidad de Sevilla. Departamento de Física Atómica, Molecular y Nuclear
Date: 2014-10
Published in: Europhysics Letters, 108 (2), 28002-p1-28002-p6.
Document type: Article
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.
Cite: López 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.
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URI: http://hdl.handle.net/11441/62537

DOI: 10.1209/0295-5075/108/28002

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