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A rupture-initiation condition expressed through the free-energy release rate of hydrogen bonds marks both the end of worm-like-chain entropic elasticity in beta-sheet domains and the onset of rupture, so strength and elasticity are coupled.
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An H-bond energy-release-rate condition sets both the entropic-elasticity limit and rupture onset
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G(x) \equiv -\frac{\partial \Delta G_{\mathrm{elastic}}}{\partial A} = G_{HB} \;\Rightarrow\; x = x_{\mathrm{limit}}
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Sinan Keten et al., “Strength limit of entropic elasticity in beta-sheet protein domains”, Physical Review E 78 (2008), doi:10.1103/physreve.78.061913; Abstract. Scope: Beta-sheet protein domains
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Sinan Keten, Markus J. Buehler. Strength limit of entropic elasticity in beta-sheet protein domains. Physical Review E 78 (2008). doi:10.1103/physreve.78.061913
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Strength limit of entropic elasticity in beta-sheet protein domains
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We show that a rupture initiation condition characterized by the free energy release rate of H-bonds characterizes the limit of WLC entropic elasticity of beta-sheet protein domains and the onset of rupture. Our findings reveal that strength and elasticity are coupled and cannot be treated separately.
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Abstract of Strength limit of entropic elasticity in beta-sheet protein domains, as read
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