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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
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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publication status
epub
subject
keywords
Auger electrons, Gas-phase biomolecules, Mass spectrometry, Protein conformation, Soft X-ray spectroscopy
in
Chemistry - A European Journal
publisher
John Wiley & Sons
external identifiers
  • scopus:85046379758
ISSN
0947-6539
DOI
10.1002/chem.201801440
language
English
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yes
id
050fd80f-34e5-4db3-99a7-dee1f6407888
date added to LUP
2018-05-17 13:43:04
date last changed
2018-05-18 03:00:02
@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},
  keyword      = {Auger electrons,Gas-phase biomolecules,Mass spectrometry,Protein conformation,Soft X-ray spectroscopy},
  language     = {eng},
  month        = {01},
  publisher    = {John Wiley & Sons},
  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},
  year         = {2018},
}