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Competition between secondary structures in gas phase polyalanines: Competition between secondary structures in gas phase polyalanines

Abstract : The temperature-dependent conformations of alanine-rich polypeptides are investi- gated using generalized ensemble Monte Carlo simulations. Pure polyalanines form α helices at low temperature, but exhibit an intermediate β-sheet structure below the coil transition. For the substituted peptide WA13 , the simulation predicts the β conformation to be more stable than helices already at low temperatures, and the β motif is further favored by entropy. Measure- ments of the electric dipole of this peptide do not provide evidence for helical structures even at room temperature. These experimental observations are thus compatible with our suggestion of β conformations, even though random-coil structures cannot be ruled out. Finally, we show how to stabilize α helices by an intense electric field, possibly leading to electrofreezing behavior.
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https://www.hal.inserm.fr/inserm-00264366
Contributor : Pierre Poulain <>
Submitted on : Monday, March 17, 2008 - 8:29:24 AM
Last modification on : Tuesday, October 27, 2020 - 2:35:49 PM

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Pierre Poulain, Florent Calvo, Rodolphe Antoine, Michel Broyer, Philippe Dugourd. Competition between secondary structures in gas phase polyalanines: Competition between secondary structures in gas phase polyalanines. EPL - Europhysics Letters, European Physical Society/EDP Sciences/Società Italiana di Fisica/IOP Publishing, 2007, 79 (6), pp.66003. ⟨10.1209/0295-5075/79/66003⟩. ⟨inserm-00264366⟩

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