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Título:
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Protein unfolding and refolding as transitions through virtual states
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Autores:
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Bonilla, L.L. ;
Carpio, Ana ;
Prados, A.
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Tipo de documento:
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texto impreso
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Editorial:
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EPL Association, European Physical Society, 2014
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias: Matemáticas
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Tipo = Artículo
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Resumen:
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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.
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En línea:
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https://eprints.ucm.es/id/eprint/29115/1/1409.7900v1.pdf
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