Competition between folded and extended structures of alanylalanine (Ala-Ala) in a molecular beam-Reference-Cited by-同舟云学术

Competition between folded and extended structures of alanylalanine (Ala-Ala) in a molecular beam

Published:2019 Issue:26 Volume:21 Page:14126-14132
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Yatsyna Vasyl¹²³⁴⁵^ORCID,Mallat Ranim¹²³^ORCID,Gorn Tim⁶⁷⁸⁹,Schmitt Michael⁶⁷⁸⁹^ORCID,Feifel Raimund¹²³^ORCID,Rijs Anouk M.⁴⁵¹⁰¹¹¹²^ORCID,Zhaunerchyk Vitali¹²³^ORCID

Affiliation:

1. University of Gothenburg

2. Department of Physics

3. Sweden

4. Radboud University

5. Institute for Molecules and Materials

6. Heinrich-Heine-Universität

7. Institut für Physikalische Chemie I

8. D-40225 Düsseldorf

9. Germany

10. FELIX Laboratory

11. 6525 ED Nijmegen

12. The Netherlands

Abstract

Structural analysis of the neutral dipeptide Ala-Ala by action spectroscopy using IRMPD-VUV spectroscopy reveals predominance of extended structure.

Funder

Horizon 2020 Framework Programme

Vetenskapsrådet

Knut och Alice Wallenbergs Stiftelse

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP00140A

Reference39 articles.

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3. Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding

4. The effect of N-methylation on the conformational landscape of alanine: the case of N-methyl-l-alanine

5. Probing the competition between secondary structures and local preferences in gas phase isolated peptide backbones

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