Journal
JOURNAL OF THE ROYAL SOCIETY INTERFACE
Volume 10, Issue 88, Pages -Publisher
ROYAL SOC
DOI: 10.1098/rsif.2013.0651
Keywords
macromolecules unfolding; biopolymers; macromolecule mechanics; protein stability; titin
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Funding
- Progetto di ricerca industriale-Regione Puglia, 'Modelli innovativi per sistemi meccatronici'
- PRIN
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We propose a simple approach, based on the minimization of the total (entropic plus unfolding) energy of a two-state system, to describe the unfolding of multidomain macromolecules (proteins, silks, polysaccharides, nanopolymers). The model is fully analytical and enlightens the role of the different energetic components regulating the unfolding evolution. As an explicit example, we compare the analytical results with a titin atomic force microscopy stretch-induced unfolding experiment showing the ability of the model to quantitatively reproduce the experimental behaviour. In the thermodynamic limit, the sawtooth force-elongation unfolding curve degenerates to a constant force unfolding plateau.
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