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

Simple item page
dc.creatorImparato, A.
dc.creatorSbrana, F.
dc.creatorVassalli, M.
dc.date2008-04-18
dc.date2008-05-29
dc.date.accessioned2026-07-07T09:41:13Z
dc.date.available2026-07-07T09:41:13Z
dc.descriptionThe 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.
dc.identifierhttps://arxiv.org/abs/0804.2980
dc.identifierhttp://arxiv.org/abs/0804.2980
dc.identifierEurophys. Lett, 82, 58006 (2008)
dc.identifierdoi:10.1209/0295-5075/82/58006
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/161754
dc.subjectSoft Condensed Matter
dc.subjectStatistical Mechanics
dc.subjectBiomolecules
dc.titleReconstructing the free energy landscape of a polyprotein by single-molecule experiments
dc.typetext

Files

Collections

arXiv