期刊
EPL
卷 82, 期 5, 页码 -出版社
EPL ASSOCIATION, EUROPEAN PHYSICAL SOCIETY
DOI: 10.1209/0295-5075/82/58006
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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. Copyright (c) EPLA, 2008.
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