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In the hierarchical Bell model applied to alpha-helices, 3–4 parallel hydrogen bonds per turn are optimal for the protein's combined mechanical and thermodynamic stability, matching the 3.6 hydrogen bonds per turn of real alpha-helices.
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Three to four parallel hydrogen bonds per turn is the mechanically and thermodynamically favoured number
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b^{*} \in \{3, 4\} \quad (\text{observed } b = 3.6 \text{ H-bonds per turn})
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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: Alpha-helical protein domains
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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 exemplify our model in a study of AHs, and show that 3-4 parallel HBs per turn are favorable in light of the protein's mechanical and thermodynamical stability, in agreement with experimental findings that AHs feature 3.6 HBs per turn.
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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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Theodor Ackbarow et al. 2007 claim: Three to four parallel hydrogen bonds per turn is the mechanically and thermodynamically favoured number
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