Indication of 310-Helix Structure in Gas-Phase Neutral Pentaalanine

Åke Andersson; Vasyl Yatsyna; Mathieu Linares; Anouk Rijs; Vitali Zhaunerchyk

doi:10.1021/acs.jpca.2c07863

Indication of 3₁₀-Helix Structure in Gas-Phase Neutral Pentaalanine

Åke Andersson, Vasyl Yatsyna, Mathieu Linares, Anouk Rijs^*, Vitali Zhaunerchyk

^*Corresponding author for this work

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

We investigate the gas-phase structure of the neutral pentaalanine peptide. The IR spectrum in the 340-1820 cm^-1 frequency range is obtained by employing supersonic jet cooling, infrared multiphoton dissociation, and vacuum-ultraviolet action spectroscopy. Comparison with quantum chemical spectral calculations suggests that the molecule assumes multiple stable conformations, mainly of two structure types. In the most stable conformation theoretically found, the N-terminus forms a C5 ring and the backbone resembles that of an 3₁₀-helix with two β-turns. Additionally, the conformational preferences of pentaalanine have been evaluated using Born-Oppenheimer molecular dynamics, showing that a nonzero simulation time step causes a systematic frequency shift.

Original language	English
Pages (from-to)	938-945
Number of pages	8
Journal	Journal of Physical Chemistry A
Volume	127
Issue number	4
Early online date	20 Jan 2023
DOIs	https://doi.org/10.1021/acs.jpca.2c07863
Publication status	Published - 2 Feb 2023

Bibliographical note

Funding Information:
We gratefully acknowledge the Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) for the support of the FELIX Laboratory. We thank the FELIX team for their experimental support and helpful discussions. The research leading to these results has received funding from the Swedish Research Council (grant no. 2019-04439). Calculations were performed with resources at the Chalmers Centre for Computational Science and Engineering (C3SE) provided by the Swedish National Infrastructure for Computing (SNIC).

Publisher Copyright:
© 2023 The Authors. Published by American Chemical Society.

Funding

We gratefully acknowledge the Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) for the support of the FELIX Laboratory. We thank the FELIX team for their experimental support and helpful discussions. The research leading to these results has received funding from the Swedish Research Council (grant no. 2019-04439). Calculations were performed with resources at the Chalmers Centre for Computational Science and Engineering (C3SE) provided by the Swedish National Infrastructure for Computing (SNIC).

Funders	Funder number
Nederlandse Organisatie voor Wetenschappelijk Onderzoek
Vetenskapsrådet	2019-04439
Vetenskapsrådet

Access to Document

10.1021/acs.jpca.2c07863

Persistent URL (handle)

Persistent link

Cite this

@article{6f9716df37174632a7c997abd4651fdf,

title = "Indication of 310-Helix Structure in Gas-Phase Neutral Pentaalanine",

abstract = "We investigate the gas-phase structure of the neutral pentaalanine peptide. The IR spectrum in the 340-1820 cm-1 frequency range is obtained by employing supersonic jet cooling, infrared multiphoton dissociation, and vacuum-ultraviolet action spectroscopy. Comparison with quantum chemical spectral calculations suggests that the molecule assumes multiple stable conformations, mainly of two structure types. In the most stable conformation theoretically found, the N-terminus forms a C5 ring and the backbone resembles that of an 310-helix with two β-turns. Additionally, the conformational preferences of pentaalanine have been evaluated using Born-Oppenheimer molecular dynamics, showing that a nonzero simulation time step causes a systematic frequency shift.",

author = "{\AA}ke Andersson and Vasyl Yatsyna and Mathieu Linares and Anouk Rijs and Vitali Zhaunerchyk",

note = "Funding Information: We gratefully acknowledge the Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) for the support of the FELIX Laboratory. We thank the FELIX team for their experimental support and helpful discussions. The research leading to these results has received funding from the Swedish Research Council (grant no. 2019-04439). Calculations were performed with resources at the Chalmers Centre for Computational Science and Engineering (C3SE) provided by the Swedish National Infrastructure for Computing (SNIC). Publisher Copyright: {\textcopyright} 2023 The Authors. Published by American Chemical Society.",

year = "2023",

month = feb,

day = "2",

doi = "10.1021/acs.jpca.2c07863",

language = "English",

volume = "127",

pages = "938--945",

journal = "Journal of Physical Chemistry A",

issn = "1089-5639",

publisher = "American Chemical Society",

number = "4",

}

TY - JOUR

T1 - Indication of 310-Helix Structure in Gas-Phase Neutral Pentaalanine

AU - Andersson, Åke

AU - Yatsyna, Vasyl

AU - Linares, Mathieu

AU - Rijs, Anouk

AU - Zhaunerchyk, Vitali

N1 - Funding Information: We gratefully acknowledge the Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) for the support of the FELIX Laboratory. We thank the FELIX team for their experimental support and helpful discussions. The research leading to these results has received funding from the Swedish Research Council (grant no. 2019-04439). Calculations were performed with resources at the Chalmers Centre for Computational Science and Engineering (C3SE) provided by the Swedish National Infrastructure for Computing (SNIC). Publisher Copyright: © 2023 The Authors. Published by American Chemical Society.

PY - 2023/2/2

Y1 - 2023/2/2

N2 - We investigate the gas-phase structure of the neutral pentaalanine peptide. The IR spectrum in the 340-1820 cm-1 frequency range is obtained by employing supersonic jet cooling, infrared multiphoton dissociation, and vacuum-ultraviolet action spectroscopy. Comparison with quantum chemical spectral calculations suggests that the molecule assumes multiple stable conformations, mainly of two structure types. In the most stable conformation theoretically found, the N-terminus forms a C5 ring and the backbone resembles that of an 310-helix with two β-turns. Additionally, the conformational preferences of pentaalanine have been evaluated using Born-Oppenheimer molecular dynamics, showing that a nonzero simulation time step causes a systematic frequency shift.

AB - We investigate the gas-phase structure of the neutral pentaalanine peptide. The IR spectrum in the 340-1820 cm-1 frequency range is obtained by employing supersonic jet cooling, infrared multiphoton dissociation, and vacuum-ultraviolet action spectroscopy. Comparison with quantum chemical spectral calculations suggests that the molecule assumes multiple stable conformations, mainly of two structure types. In the most stable conformation theoretically found, the N-terminus forms a C5 ring and the backbone resembles that of an 310-helix with two β-turns. Additionally, the conformational preferences of pentaalanine have been evaluated using Born-Oppenheimer molecular dynamics, showing that a nonzero simulation time step causes a systematic frequency shift.

UR - http://www.scopus.com/inward/record.url?scp=85146873908&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85146873908&partnerID=8YFLogxK

U2 - 10.1021/acs.jpca.2c07863

DO - 10.1021/acs.jpca.2c07863

M3 - Article

C2 - 36669091

AN - SCOPUS:85146873908

SN - 1089-5639

VL - 127

SP - 938

EP - 945

JO - Journal of Physical Chemistry A

JF - Journal of Physical Chemistry A

IS - 4

ER -