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Soft X-ray Spectroscopy as a Probe for Gas-Phase Protein Structure : Electron Impact Ionization from Within

Bari, Sadia ; Egorov, Dmitrii ; Jansen, Thomas L.C. ; Boll, Rebecca ; Hoekstra, Ronnie ; Techert, Simone ; Zamudio-Bayer, Vicente ; Bülow, Christine ; Lindblad, Rebecka LU and Leistner, Georg , et al. (2018) In Chemistry - A European Journal 24(30). p.7631-7636
Abstract

Preservation of protein conformation upon transfer into the gas phase is key for structure determination of free single molecules, for example using X-ray free-electron lasers. In the gas phase, the helicity of melittin decreases strongly as the protein's protonation state increases. We demonstrate the sensitivity of soft X-ray spectroscopy to the gas-phase structure of melittin cations ([melittin+qH]q+, q=2-4) in a cryogenic linear radiofrequency ion trap. With increasing helicity, we observe a decrease of the dominating carbon 1s-π* transition in the amide C=O bonds for non-dissociative single ionization and an increase for non-dissociative double ionization. As the underlying mechanism we identify inelastic electron... (More)

Preservation of protein conformation upon transfer into the gas phase is key for structure determination of free single molecules, for example using X-ray free-electron lasers. In the gas phase, the helicity of melittin decreases strongly as the protein's protonation state increases. We demonstrate the sensitivity of soft X-ray spectroscopy to the gas-phase structure of melittin cations ([melittin+qH]q+, q=2-4) in a cryogenic linear radiofrequency ion trap. With increasing helicity, we observe a decrease of the dominating carbon 1s-π* transition in the amide C=O bonds for non-dissociative single ionization and an increase for non-dissociative double ionization. As the underlying mechanism we identify inelastic electron scattering. Using an independent atom model, we show that the more compact nature of the helical protein conformation substantially increases the probability for off-site intramolecular ionization by inelastic Auger electron scattering.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Auger electrons, Gas-phase biomolecules, Mass spectrometry, Protein conformation, Soft X-ray spectroscopy
in
Chemistry - A European Journal
volume
24
issue
30
pages
7631 - 7636
publisher
Wiley-Blackwell
external identifiers
  • scopus:85046379758
  • pmid:29637635
ISSN
0947-6539
DOI
10.1002/chem.201801440
language
English
LU publication?
yes
id
050fd80f-34e5-4db3-99a7-dee1f6407888
date added to LUP
2018-05-17 13:43:04
date last changed
2024-03-18 09:35:18
@article{050fd80f-34e5-4db3-99a7-dee1f6407888,
  abstract     = {{<p>Preservation of protein conformation upon transfer into the gas phase is key for structure determination of free single molecules, for example using X-ray free-electron lasers. In the gas phase, the helicity of melittin decreases strongly as the protein's protonation state increases. We demonstrate the sensitivity of soft X-ray spectroscopy to the gas-phase structure of melittin cations ([melittin+qH]<sup>q+</sup>, q=2-4) in a cryogenic linear radiofrequency ion trap. With increasing helicity, we observe a decrease of the dominating carbon 1s-π* transition in the amide C=O bonds for non-dissociative single ionization and an increase for non-dissociative double ionization. As the underlying mechanism we identify inelastic electron scattering. Using an independent atom model, we show that the more compact nature of the helical protein conformation substantially increases the probability for off-site intramolecular ionization by inelastic Auger electron scattering.</p>}},
  author       = {{Bari, Sadia and Egorov, Dmitrii and Jansen, Thomas L.C. and Boll, Rebecca and Hoekstra, Ronnie and Techert, Simone and Zamudio-Bayer, Vicente and Bülow, Christine and Lindblad, Rebecka and Leistner, Georg and Ławicki, Arkadiusz and Hirsch, Konstantin and Miedema, Piter S. and vonIssendorff, Bernd and Lau, J. Tobias and Schlathölter, Thomas}},
  issn         = {{0947-6539}},
  keywords     = {{Auger electrons; Gas-phase biomolecules; Mass spectrometry; Protein conformation; Soft X-ray spectroscopy}},
  language     = {{eng}},
  month        = {{05}},
  number       = {{30}},
  pages        = {{7631--7636}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Chemistry - A European Journal}},
  title        = {{Soft X-ray Spectroscopy as a Probe for Gas-Phase Protein Structure : Electron Impact Ionization from Within}},
  url          = {{http://dx.doi.org/10.1002/chem.201801440}},
  doi          = {{10.1002/chem.201801440}},
  volume       = {{24}},
  year         = {{2018}},
}