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  Soft X-ray spectroscopy as a probe for gas-phase protein structure: Electron impact ionization from within.

Bari, S., Egorov, D., Jansen, T. L., Boll, R., Hoekstra, R., Techert, S., et al. (2018). Soft X-ray spectroscopy as a probe for gas-phase protein structure: Electron impact ionization from within. Chemistry - A European Journal, 24(30), 7631-7636. doi:10.1002/chem.201801440.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-28CD-C Version Permalink: http://hdl.handle.net/21.11116/0000-0003-2F1B-C
Genre: Journal Article

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 Creators:
Bari, S.1, Author              
Egorov, D., Author
Jansen, T. L.C., Author
Boll, R.1, Author              
Hoekstra, R., Author
Techert, S.1, Author              
Zamudio-Bayer, V., Author
Bülow, C., Author
Lindblad, R., Author
Leistner, G., Author
Lawicki, A., Author
Hirsch, K., Author
Miedema, P. S., Author
von Issendorf, B., Author
Lau, T., Author
Schlathölter, T., Author
Affiliations:
1Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society, ou_578564              

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Free keywords: Auger electrons; gas-phase biomolecules; mass spectrometry; protein conformation; soft X-ray spectroscopy
 Abstract: Preservation of protein conformation upon transfer into the gas‐phase is key for structure determination of free single molecules, e.g. 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 conformation 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‐* 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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Language(s): eng - English
 Dates: 2018-04-102018-05-28
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/chem.201801440
 Degree: -

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Title: Chemistry - A European Journal
Source Genre: Journal
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Pages: - Volume / Issue: 24 (30) Sequence Number: - Start / End Page: 7631 - 7636 Identifier: -