| Issue |
EPL
Volume 108, Number 2, October 2014
|
|
|---|---|---|
| Article Number | 28002 | |
| Number of page(s) | 6 | |
| Section | Interdisciplinary Physics and Related Areas of Science and Technology | |
| DOI | https://doi.org/10.1209/0295-5075/108/28002 | |
| Published online | 14 October 2014 | |
Protein unfolding and refolding as transitions through virtual states
1 G. Millán Institute, Fluid Dynamics, Nanoscience and Industrial Mathematics, Universidad Carlos III de Madrid E-28911, Leganés, Spain
2 Departamento de Matemática Aplicada, Universidad Complutense de Madrid - E-28040, Madrid, Spain
3 Física Teórica, Universidad de Sevilla - Apartado de Correos 1065, E-41080, Sevilla, Spain
Received: 24 May 2014
Accepted: 26 September 2014
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.
PACS: 87.15.Cc – Folding: thermodynamics, statistical mechanics, models, and pathways / 05.40.-a – Fluctuation phenomena, random processes, noise, and Brownian motion / 87.14.et – Generic models (lattice, HP, etc.)
© EPLA, 2014
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