Article
Protein unfolding and refolding as transitions through virtual states
Author/s | López Bonilla, Luis
Carpio Rodríguez, Ana Prados Montaño, Antonio |
Department | Universidad de Sevilla. Departamento de Física Atómica, Molecular y Nuclear |
Publication Date | 2014-10 |
Deposit Date | 2017-07-14 |
Published in |
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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 ... 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. |
Funding agencies | Ministerio de Economía y Competitividad (MINECO). España |
Project ID. | info:eu-repo/grantAgreement/MINECO/FIS2011-28838-C02-01
info:eu-repo/grantAgreement/MINECO/FIS2011-28838-C02-02 info:eu-repo/grantAgreement/MINECO/FIS2011-24460 |
Citation | 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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