Globule to Helix Transition in Sodiated Polyalanines

Abstract : The structures of sodiated poly-alanine peptides containing 8-12 residues are investigated using infrared multiple photon dissociation (IRMPD) spectroscopy and classical and quantum modeling. Calculations indicate that the a-helical structure is the most stable conformation for the peptides whatever their size. The IRMPD spectra provide evidence for the coexistence of helical and globular shapes for Ala(8)Na(+), and possibly for Ala(9)Na(+) The turning point from globule to helix is thus found at Ala(8-9)Na(+). The N-H and O-H stretching region allows identifying a new spectroscopic pattern typical for alpha-helical structures of polyalanines.
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Submitted on : Friday, November 29, 2013 - 2:31:02 PM
Last modification on : Wednesday, November 20, 2019 - 2:52:24 AM

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Jonathan K. Martens, Isabelle Compagnon, Edith Nicol, Terry B. Mcmahon, Carine Clavaguera, et al.. Globule to Helix Transition in Sodiated Polyalanines. Journal of Physical Chemistry Letters, American Chemical Society, 2012, 3 (22), pp.3320-3324. ⟨10.1021/jz301326w⟩. ⟨hal-00904399⟩

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