Soft X-ray Spectroscopy as a Probe for Gas-Phase Protein Structure : Electron Impact Ionization from Within
(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.
(Less)
- author
- organization
- publishing date
- 2018-05-28
- 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
-
- pmid:29637635
- scopus:85046379758
- 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
- 2024-07-08 14:03:07
@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}}, }