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The deviations of beta-sheet protein domains from ideal worm-like-chain elasticity seen in force spectroscopy are explained by a model with two generic parameters, the H-bond energy and the backbone persistence length.
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Notation basis: The WLC interpolation formula is the standard one the abstract names; the two-parameter limit condition is stated in words (next claim) and its explicit form is in the full text, not vendored.
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Two parameters explain the breakdown of worm-like-chain elasticity in beta-sheet domains
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F_{\mathrm{WLC}}(x) = \frac{k_B T}{\xi_p}\left[\frac{1}{4(1 - x/L)^2} - \frac14 + \frac{x}{L}\right];\quad \text{model parameters } (E_{HB}, \xi_p)
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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 under tension
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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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Here we report a simple model that explains the physical mechanism that leads to the breakdown of the WLC idealization in experiments by using only two generic parameters of the protein domain, the H-bond energy and the protein backbone's persistence length.
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Abstract of Strength limit of entropic elasticity in beta-sheet protein domains, as read
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