The DOI matches its Crossref record; 163 of the 163 references it cites were found in a registry or an index.
The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics
Abstract
Mass spectrometry is a vital tool for molecular characterization, and the allied technique of ion mobility is enhancing many areas of (bio)chemical analysis. Strong synergy arises between these two techniques because of their ability to ascertain complementary information about gas-phase ions. Ion mobility separates ions (from small molecules up to megadalton protein complexes) based on their differential mobility through a buffer gas. Ion mobility-mass spectrometry (IM-MS) can thus act as a tool to separate complex mixtures, to resolve ions that may be indistinguishable by mass spectrometry alone, or to determine structural information (for example rotationally averaged cross-sectional area), complementary to more traditional structural approaches. Finally, IM-MS can be used to gain insights into the conformational dynamics of a system, offering a unique means of characterizing flexibility and folding mechanisms. This Review critically describes how IM-MS has been used to enhance various areas of chemical and biophysical analysis.
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“Previous studies have shown that IM-MS correlates with known protein structure,”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [24]
In the citing paper
“Ion mobility experiments show that the overall 3D shape of proteins – especially in the lower charge states naturally generated by ESI from non-denaturing solutions – is usually consistent with structures obtained from X-ray diffraction (XRD) and nuclear magnetic resonance (NMR) (although exceptions exist).”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [24]
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Schrimpe‐Rutledge, A. C., Codreanu, S. G., Sherrod, S. D., & MCLEAN, J. A. J. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1469-y · Cited by 1,447
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Metadata
- Authors
- Lanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E.
- Affiliations
- University of Liverpool (GB)
- University of Manchester (GB)
- Corresponding author
- Eyers, Claire E.
- Venue
- Nature Chemistry
- Published
- 2014-03-21
- Volume
- 6
- Issue
- 4
- Pages
- 281-294
- ISSN
- 1755-4330 (ISSN-L)
- 1755-4349
- OpenAlex
- W1992505804
- Cited by
- 901
- References
- 163
- Citations by year
- 2026: 28 · 2025: 58 · 2024: 50 · 2023: 60 · 2022: 67 · 2021: 79 · 2020: 92 · 2019: 92 · 2018: 100 · 2017: 108 · 2016: 85 · 2015: 56 · 2014: 24
- FWCI
- 8.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- European Commission
- Biotechnology and Biological Sciences Research Council (BB/H007113/1, BB/F00561X/1, BB/G009058/1)
- 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
- ion mobility mass spectrometry, structural characterization, conformational dynamics, cross-sectional area, complex mixtures, protein flexibility, protein folding mechanism, molecular characterization
- MeSH terms
- Biophysics, Ions, Molecular Conformation, Mass Spectrometry
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