Reconstructing the free-energy landscape of a polyprotein by single-molecule experiments

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
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Vassalli, Dr 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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