Charge‐Induced Unzipping of Isolated Proteins to a Defined Secondary Structure
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Here we present a combined experimental and theoretical study on the secondary structure of isolated proteins as a function of charge state. In infrared spectra of the proteins ubiquitin and cytochrome c, amide I (C=O stretch) and amide II (N–H bend) bands can be found at positions that are typical for condensed‐phase proteins. For high charge states a new band appears, substantially red‐shifted from the amide II band observed at lower charge states. The observations are interpreted in terms of Coulomb‐driven transitions in secondary structures from mostly helical to extended C 5 ‐type hydrogen‐bonded structures. Support for this interpretation comes from simple energy considerations as well as from quantum chemical calculations on model peptides. This transition in secondary structure is most likely universal for isolated proteins that occur in mass spectrometric experiments.
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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 [173]
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Formation of Neutral Peptide Aggregates as Studied by Mass‐Selective IR Action Spectroscopy
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Infrared fingerprints of water collective dynamics indicate proton transport in biological systems
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Cryogenic Infrared Spectroscopy Unmasks Gas‐Phase Charge Migration in Mucin‐Type O ‐Glycans
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Sohail, A., Tarasov, A. S., Degterev, A. E., Degtereva, M. M., Pavlova, M., Khorshev, N. A., Levin, Y., Анатольевич, Л. И., & Tarasov, S. A. (2026) · Micromachines · doi:10.3390/mi17101174
- Authors
- González Flórez, A. I., Mucha, E., Ahn, D., Gewinner, S., Schöllkopf, W., Pagel, K., & von Helden, G.
- Affiliations
- Fritz-Haber-Institut der Max-Planck-Gesellschaft Faradayweg 4–6 14195 Berlin Germany
- Fritz Haber Institute of the Max Planck Society (DE)
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2016-02-05
- Volume
- 55
- Issue
- 10
- Pages
- 3295-3299
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- PMC
- PMC4770441
- OpenAlex
- W2239839812
- Cited by
- 79
- References
- 23
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 5 · 2023: 7 · 2022: 4 · 2021: 11 · 2020: 6 · 2019: 3 · 2018: 16 · 2017: 7 · 2016: 9
- FWCI
- 5.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Angewandte Chemie International Edition (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, cc-by-nc)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- protein secondary structure, isolated proteins, high charge states, ubiquitin, cytochrome c, amide I band, amide II band, hydrogen-bonded structure, protein mass spectrometry, infrared spectra, model peptides
- MeSH terms
- Hydrogen Bonding, Spectrophotometry, Infrared, Protein Structure, Secondary, Ubiquitin, Cytochromes c
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