Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study
Open accessAbstract
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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Infrared ion spectroscopy has already been demonstrated on small monomeric proteins.
“Infrared ion spectroscopy has already been demonstrated on small monomeric proteins.32,173”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [32]
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- Authors
- Seo, J., Hoffmann, W., Warnke, S., Bowers, M. T., Pagel, K., & von Helden, G.
- Affiliations
- Fritz Haber Institute of the Max Planck Society (DE)
- University of California, Santa Barbara (US)
- Fritz-Haber-Institut der Max-Planck-Gesellschaft Faradayweg 4–6 14195 Berlin Germany
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2016-08-22
- Volume
- 55
- Issue
- 45
- Pages
- 14173-14176
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- PMC
- PMC5113788
- OpenAlex
- W2517160828
- Cited by
- 132
- References
- 36
- Citations by year
- 2026: 3 · 2025: 11 · 2024: 10 · 2023: 11 · 2022: 8 · 2021: 14 · 2020: 15 · 2019: 26 · 2018: 15 · 2017: 17 · 2016: 2
- FWCI
- 9.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Angewandte Chemie International Edition (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Open Access System for Information Sharing (Pohang University of Science and Technology) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- National Science Foundation (CHE-1301032)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Molecular Spectroscopy and Structure
- Keywords
- gas-phase protein structure, ion mobility mass spectrometry, infrared spectroscopy, myoglobin, β-lactoglobulin, secondary structure, protein tertiary structure, helical proteins, beta-sheet proteins
- MeSH terms
- Lactoglobulins, Models, Molecular, Myoglobin, Protein Conformation, Solvents, Mass Spectrometry
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