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  Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study

Seo, J., Hoffmann, W., Warnke, S., Bowers, M. T., Pagel, K., & Helden, G. v. (2016). Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study. Angewandte Chemie International Edition, 55(45), 14173-14176. doi:10.1002/anie.201606029.

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Seo_et_al-2016-Angewandte_Chemie_International_Edition.pdf (Publisher version), 2MB
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Seo_et_al-2016-Angewandte_Chemie_International_Edition.pdf
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2016
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2016 The Authors. Published by Wiley-VCH VerlagGmbH &Co. KGaA,Weinheim

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 Creators:
Seo, Jongcheol1, Author              
Hoffmann, Waldemar1, Author              
Warnke, Stephan1, Author              
Bowers, Michael T.2, Author
Pagel, Kevin1, 3, Author              
Helden, Gert von1, Author              
Affiliations:
1Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
2Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106, USA, ou_persistent22              
3Institut für Chemie und Biochemie der Freien Universität Berlin, Takustrasse 3, 14195 Berlin (Germany), ou_persistent22              

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 Abstract: Can the structures of small to medium-sized proteins be conserved after transfer from the solution phase to the gas phase? A large number of studies have been devoted to this topic, however the answer has not been unambiguously determined to date. A clarification of this problem is important since it would allow very sensitive native mass spectrometry techniques to be used to address problems relevant to structural biology. A combination of ion-mobility mass spectrometry with infrared spectroscopy was used to investigate the secondary and tertiary structure of proteins carefully transferred from solution to the gas phase. The two proteins investigated are myoglobin and β-lactoglobulin, which are prototypical examples of helical and β-sheet proteins, respectively. The results show that for low charge states under gentle conditions, aspects of the native secondary and tertiary structure can be conserved.

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 Dates: 2016-06-212016-10-282016-11-02
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201606029
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Title: Angewandte Chemie International Edition
  Other : Angew. Chem., Int. Ed.
  Other : Angew. Chem. Int. Ed.
  Other : Angewandte Chemie, International Edition
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: 4 Volume / Issue: 55 (45) Sequence Number: - Start / End Page: 14173 - 14176 Identifier: ISSN: 1433-7851
CoNE: https://pure.mpg.de/cone/journals/resource/1433-7851