Protein unfolding and refolding as transitions through virtual states



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Bonilla, L.L. and Carpio, Ana and Prados, A. (2014) Protein unfolding and refolding as transitions through virtual states. EPL, 108 (2). ISSN 0295-5075

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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.

Item Type:Article
Uncontrolled Keywords:PACS 87.15.Cc –Folding: thermodynamics, statistical mechanics, models, and pathways PACS 05.40.-a – Fluctuation phenomena, random processes, noise, and Brownian motion PACS – Generic models (lattice, HP, etc.)
Subjects:Sciences > Mathematics
ID Code:29115
Deposited On:09 Mar 2015 11:40
Last Modified:12 Dec 2018 15:06

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