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Issue 7, 2015
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Native like helices in a specially designed β peptide in the gas phase

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Abstract

In the natural peptides, helices are stabilized by hydrogen bonds that point backward along the sequence direction. Until now, there is only little evidence for the existence of analogous structures in oligomers of conformationally unrestricted β amino acids. We specifically designed the β peptide Ac-(β2hAla)6-LysH+ to form native like helical structures in the gas phase. The design follows the known properties of the peptide Ac-Ala6-LysH+ that forms a α helix in isolation. We perform ion-mobility mass-spectrometry and vibrational spectroscopy in the gas phase, combined with state-of-the-art density-functional theory simulations of these molecular systems in order to characterize their structure. We can show that the straightforward exchange of alanine residues for the homologous β amino acids generates a system that is generally capable of adopting native like helices with backward oriented H-bonds. By pushing the limits of theory and experiments, we show that one cannot assign a single preferred structure type due to the densely populated energy landscape and present an interpretation of the data that suggests an equilibrium of three helical structures.

Graphical abstract: Native like helices in a specially designed β peptide in the gas phase

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Publication details

The article was received on 10 Nov 2014, accepted on 07 Jan 2015 and first published on 09 Jan 2015


Article type: Paper
DOI: 10.1039/C4CP05216A
Citation: Phys. Chem. Chem. Phys., 2015,17, 5376-5385
  • Open access: Creative Commons BY license
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    Native like helices in a specially designed β peptide in the gas phase

    F. Schubert, K. Pagel, M. Rossi, S. Warnke, M. Salwiczek, B. Koksch, G. von Helden, V. Blum, C. Baldauf and M. Scheffler, Phys. Chem. Chem. Phys., 2015, 17, 5376
    DOI: 10.1039/C4CP05216A

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