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Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons22084

Schubert,  Franziska
Theory, Fritz Haber Institute, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons32738

Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Institut für Chemie und Biochemie, Freie Universität Berlin;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons21421

Rossi,  Mariana
Theory, Fritz Haber Institute, Max Planck Society;
Physical and Theoretical Chemistry Laboratory, University of Oxford;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons22220

Warnke,  Stephan
Molecular Physics, Fritz Haber Institute, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons21614

Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons21379

Blum,  Volker
Theory, Fritz Haber Institute, Max Planck Society;
Duke University, MEMS Department, Durham, NC 27708, USA;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons21325

Baldauf,  Carsten
Theory, Fritz Haber Institute, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons22064

Scheffler,  Matthias
Theory, Fritz Haber Institute, Max Planck Society;

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Fulltext (public)

c4cp05216a.pdf
(Publisher version), 3MB

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Citation

Schubert, F., Pagel, K., Rossi, M., Warnke, S., Salwiczek, M., Koksch, B., et al. (2015). Native like helices in a specially designed β peptide in the gas phase. Physical Chemistry Chemical Physics, 17(7), 5376-5385. doi:10.1039/C4CP05216A.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-C332-1
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.