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At fast pulling rates alpha-helical and beta-sheet domains unfold by sequential rupture of individual hydrogen bonds; at slow pulling rates they unfold by simultaneous rupture of several hydrogen bonds.
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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 and beta-sheet domains in atomistic simulation
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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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Whereas the unfolding mechanism at fast pulling rates is sequential rupture of individual hydrogen bonds (HBs), unfolding at slow pulling rates proceeds by simultaneous rupture of several HBs.
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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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