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A hierarchical Bell model, which extends Bell's rate theory of bond rupture to explicitly include the hierarchical architecture of a protein (how many H-bonds break together and how they are arranged), gives a structure–property relationship for the strength of protein domains.
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Notation basis: The abstract names the model and says it derives from Bell's theory; the Bell force–rate form written here is the standard one the model extends. The hierarchical form (how E_b and x_b scale with b) is in the full text, which is not vendored, so it is not written here.
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The hierarchical Bell model: a structure–property law for protein strength
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F(v) = \frac{k_B T}{x_b}\,\ln\frac{v}{v_0} + \frac{E_b}{x_b}, \quad E_b,\ x_b \text{ set by the number } b \text{ of H-bonds rupturing together}
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Theodor Ackbarow et al., “Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains”, Proceedings of the National Academy of Sciences 104, 16410-16415 (2007), doi:10.1073/pnas.0705759104; Abstract. Scope: Protein domains whose strength is set by clustered H-bond rupture
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Theodor Ackbarow, Xuefeng Chen, Sinan Keten, Markus J. Buehler. Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains. Proceedings of the National Academy of Sciences 104, 16410-16415 (2007). doi:10.1073/pnas.0705759104
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Theodor Ackbarow, Xuefeng Chen, Sinan Keten, Markus J. Buehler
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Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains
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We derive the hierarchical Bell model, a theory that explicitly considers the hierarchical architecture of proteins, providing a rigorous structure-property relationship.
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Abstract of Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of α-helical and β-sheet protein domains, as read
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