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In coiled-coil proteins under tension the alpha-to-beta transition is controlled by alpha-helix length: in the asymptotic limit, helices shorter than 26 amino acids or 3.8 nm slide past each other, whereas longer ones undergo the alpha-to-beta transition.
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Notation basis: Threshold stated in the abstract; the derivation (balance of sliding versus unfolding energy) is in the full text.
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Alpha-helices shorter than 26 residues (3.8 nm) slide; longer ones convert to beta-sheet under stretch
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L^{*} = 26\ \text{residues} \approx 3.8\ \mathrm{nm}:\quad L < L^{*} \Rightarrow \text{sliding},\ L > L^{*} \Rightarrow \alpha\to\beta
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Zhao Qin et al., “Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale”, Physical Review Letters 104 (2010), doi:10.1103/physrevlett.104.198304; Abstract. Scope: Alpha-helical coiled-coil proteins of varying length under stretch (MD and theory)
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Zhao Qin, Markus J. Buehler. Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale. Physical Review Letters 104 (2010). doi:10.1103/physrevlett.104.198304
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Molecular Dynamics Simulation of theα-Helix toβ-Sheet Transition in Coiled Protein Filaments: Evidence for a Critical Filament Length Scale
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In the asymptotic limit, short proteins with less than 26 amino acids or 3.8 nm length reveal interprotein sliding, whereas proteins with greater lengths feature an α-β transition, leading to a significant increase in the protein's stiffness, strength, and energy dissipation capacity at large deformation.
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Zhao Qin et al. 2010 claim: Alpha-helices shorter than 26 residues (3.8 nm) slide; longer ones convert to beta-sheet under stretch
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