Imparato, A., Sbrana, F. and Vassalli, M. (2008) Reconstructing the free-energy landscape of a polyprotein by single-molecule experiments. EPL (Europhysics Letters), 82(5), 58006. (doi: 10.1209/0295-5075/82/58006)
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Abstract
The mechanical unfolding of an engineered protein composed of eight domains of Ig27 is investigated by using atomic force microscopy. Exploiting a fluctuation relation, the equilibrium free energy as a function of the molecule elongation is estimated from pulling experiments. Such a free energy exhibits a regular shape that sets a typical unfolding length at zero force of the order of 20 nm. This length scale turns out to be much larger than the kinetic-unfolding length that is also estimated by analyzing the typical rupture force of the molecule under dynamic loading.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Vassalli, Professor Massimo |
Authors: | Imparato, A., Sbrana, F., and Vassalli, M. |
College/School: | College of Science and Engineering > School of Engineering > Biomedical Engineering |
Journal Name: | EPL (Europhysics Letters) |
Publisher: | IOP Publishing |
ISSN: | 0295-5075 |
ISSN (Online): | 1286-4854 |
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