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

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Seo,  Jongcheol
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Hoffmann,  Waldemar
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Warnke,  Stephan
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Institut für Chemie und Biochemie der Freien Universität Berlin;

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Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-BE39-1
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.