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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]
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“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]
Citations
Cites
Aerosol classification by electric mobility: apparatus, theory, and applications
Knutson, E. O., & WHITBY, K. T. (1975) · Journal of Aerosol Science · doi:10.1016/0021-8502(75)90060-9 · Cited by 1,461
Bernstein, S. L., Dupuis, N., Lazo, N. D., Wyttenbach, T., Condron, M. M., Bitan, G., Teplow, D. B., Shea, J., Ruotolo, B. T., Robinson, C. V., et al. (2009) · Nature Chemistry · doi:10.1038/nchem.247 · Cited by 943
An exact hard-spheres scattering model for the mobilities of polyatomic ions
Shvartsburg, A. A., & Jarrold, M. F. (1996) · Chemical Physics Letters · doi:10.1016/0009-2614(96)00941-4 · Cited by 813
Bush, M. F., Hall, Z., Giles, K., Hoyes, J. B., Robinson, C. V., & Ruotolo, B. T. (2010) · Analytical Chemistry · doi:10.1021/ac1022953 · Cited by 798
Kantardjieff, K. A., & Rupp, B. (2003) · Protein Science · doi:10.1110/ps.0350503 · Cited by 769
Native mass spectrometry: a bridge between interactomics and structural biology
Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766
Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
Picotti, P., Bodenmiller, B., Mueller, L. N., Domon, B., & Aebersold, R. (2009) · Cell · doi:10.1016/j.cell.2009.05.051 · Cited by 744
Applications of a travelling wave‐based radio‐frequency‐only stacked ring ion guide
Giles, K., Pringle, S. D., Worthington, K. R., Little, D., Wildgoose, J. L., & Bateman, R. H. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1641 · Cited by 730
Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses‐ A Review
Ranjbar, B., & Gill, P. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00847.x · Cited by 704
Definitions of terms relating to mass spectrometry (IUPAC Recommendations 2013)
Murray, K. K., Boyd, R. K., Eberlin, M. N., Langley, G. J., Li, L., & Naito, Y. (2013) · Pure and Applied Chemistry · doi:10.1351/pac-rec-06-04-06 · Cited by 690
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Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000
Meier, F., Brunner, A., Koch, S., Koch, H., Lubeck, M., Krause, M., Goedecke, N., Decker, J., Kosinski, T., Park, M. A., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.000900 · Cited by 971
Čajka, T., & Fiehn, O. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04491 · Cited by 839
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Jena, P., & Sun, Q. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00524 · Cited by 676
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“Perhaps even more convincing arguments that protein structures can be partly retained in the gas phase come from more recent ion mobility spectrometry (IMS) experiments [62, 63].”
BackgroundMetabolite Measurement: Pitfalls to Avoid and Practices to Follow
Lu, W., Su, X., Klein, M. S., Lewis, I. A., Fiehn, O., & Rabinowitz, J. D. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044952 · Cited by 467
Ion Mobility-Mass Spectrometry: Time-Dispersive Instrumentation
May, J. C., & MCLEAN, J. A. J. (2014) · Analytical Chemistry · doi:10.1021/ac504720m · Cited by 444
Meier, F., Beck, S., Graßl, N., Lubeck, M., Park, M. A., Raether, O., & Mann, M. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00932 · Cited by 439
de Souza, L. P., Alseekh, S., Scossa, F., & Fernie, A. R. (2021) · Nature Methods · doi:10.1038/s41592-021-01116-4 · Cited by 381
Trapped ion mobility spectrometry: A short review
Ridgeway, M. E., Lubeck, M., Jordens, J., Mann, M., & Park, M. A. (2018) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2018.01.006 · Cited by 306
Advances in mass spectrometry-based metabolomics for investigation of metabolites
Ren, J., Zhang, A., Kong, L. D., & Wang, X. (2018) · RSC Advances · doi:10.1039/c8ra01574k · Cited by 311
Palaniappan, K. K., & Bertozzi, C. R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00023 · Cited by 280
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Paglia, G., & Astarita, G. (2017) · Nature Protocols · doi:10.1038/nprot.2017.013 · Cited by 255
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Dixit, S. M., Polasky, D. A., & Ruotolo, B. T. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.11.010 · Cited by 235
“charge ratio and reports ion size in terms of an orientationally-averaged collision cross section (CCS), has also been widely deployed in combination with MS as a platform for structural biology [5].”
MethodDeng, L., Webb, I., Garimella, S., Hamid, A. M., Zheng, X., Norheim, R. V., Prost, S. A., Anderson, G., Sandoval, J. A., Baker, E. S., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00185 · Cited by 229
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Lössl, P., van de Waterbeemd, M., & Heck, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694818 · Cited by 222
Ruan, T., Li, P., Wang, H., Li, T., & Jiang, G. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00056 · Cited by 224
Zhou, Z., Shen, X., Tu, J., & Zhu, Z. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03091 · Cited by 210
Ion Mobility Spectrometry in Food Analysis: Principles, Current Applications and Future Trends
Hernández‐Mesa, M., Ropartz, D., García-Campaña, A. M., Rogniaux, H., Dervilly, G., & Bizec, B. L. (2019) · Molecules · doi:10.3390/molecules24152706 · Cited by 203
Zheng, X., Aly, N. A., Zhou, Y., Dupuis, K. T., Pena, A. B., Paurus, V., Orton, D., Wilson, R., Payne, S., Smith, R. D., et al. (2017) · Chemical Science · doi:10.1039/c7sc03464d · Cited by 200
Pérez‐Riverol, Y., Alpi, E., Wang, R., Hermjakob, H., & Vizcaíno, J. A. (2014) · PROTEOMICS · doi:10.1002/pmic.201400302 · Cited by 202
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Largy, E., Mergny, J., & Gabelica, V. (2016) · Metal ions in life sciences · doi:10.1007/978-3-319-21756-7_7 · Cited by 193
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Gray, C., Migas, L. G., Barran, P. E., Pagel, K., Seeberger, P. H., Eyers, C. E., Boons, G., Pohl, N. L. B., Compagnon, I., Widmalm, G., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06406 · Cited by 187
Self-citationAdding a new separation dimension to MS and LC–MS: What is the utility of ion mobility spectrometry?
D’Atri, V., Causon, T. J., Hernandez‐Alba, O., Mutabazi, A., Veuthey, J., Cianférani, S., & Guillarme, D. (2017) · Journal of Separation Science · doi:10.1002/jssc.201700919 · Cited by 192
Ion Mobility Collision Cross Section Compendium
May, J. C., Morris, C. B., & MCLEAN, J. A. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04905 · Cited by 183
Plants Metabolome Study: Emerging Tools and Techniques
Patel, M. K., Pandey, S., Kumar, M., Haque, M. R., Pal, S., & Yadav, N. S. (2021) · Plants · doi:10.3390/plants10112409 · Cited by 185
Cumeras, R., Figueras, E., Davis, C. E., Baumbach, J., & Gràcia, I. (2014) · The Analyst · doi:10.1039/c4an01101e · Cited by 173
Gerhardt, N., Birkenmeier, M., Sanders, D., Rohn, S., & Weller, P. (2017) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-017-0338-2 · Cited by 166
Yao, W., Cai, Y., Liu, D., Chen, Y., Li, J., Zhang, M., Chen, N., & Zhang, H. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130989 · Cited by 162
Dias, D. A., Jones, O. A. H., Beale, D. J., Boughton, B. A., Benheim, D., Kouremenos, K. A., Wolfender, J., & Wishart, D. S. (2016) · Metabolites · doi:10.3390/metabo6040046 · Cited by 168
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Covington, B. C., MCLEAN, J. A. J., & Bachmann, B. O. (2016) · Natural Product Reports · doi:10.1039/c6np00048g · Cited by 154
Zhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146
Applications of ion mobility mass spectrometry for high throughput, high resolution glycan analysis
Gray, C., Thomas, B., Upton, R., Migas, L. G., Eyers, C. E., Barran, P. E., & Flitsch, S. L. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.02.003 · Cited by 149
Self-citationHernández‐Mesa, M., Escourrou, A., Monteau, F., Bizec, B. L., & Dervilly, G. (2017) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2017.07.006 · Cited by 145
Pičmanová, M., Neilson, E. H. J., Motawia, M. S., Olsen, C. E., Agerbirk, N., Gray, C., Flitsch, S. L., Meier, S., Silvestro, D., Jørgensen, K., et al. (2015) · Biochemical Journal · doi:10.1042/bj20150390 · Cited by 142
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Reading, E., Liko, I., Allison, T. M., Benesch, J. L. P., Laganowsky, A., & Robinson, C. V. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201411622 · Cited by 137
Extraction Systems and Analytical Techniques for Food Phenolic Compounds: A Review
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Seo, J., Hoffmann, W., Warnke, S., Bowers, M. T., Pagel, K., & von Helden, G. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201606029 · Cited by 132
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Po, A., & Eyers, C. E. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00416 · Cited by 117
Self-citationChen, S., & Russell, D. H. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1191-1 · Cited by 113
Allen, S., Giles, K., Gilbert, T., & Bush, M. F. (2016) · The Analyst · doi:10.1039/c5an02107c · Cited by 113
Paszkiewicz, M., Godlewska, K., Lis, H., Caban, M., Białk‐Bielińska, A., & Stepnowski, P. (2022) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2022.116671 · Cited by 112
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Xie, T., Guo, K., Guo, Z., Gao, W., Wojtas, Ł., Ning, G., Huang, M., Lu, X., Li, J., Liao, S., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201503609 · Cited by 108
Yang, X., Wei, S., Liu, B., Guo, D., Zheng, B.-X., Feng, L., Liu, Y., Tomás-Barberán, F. A., Luo, L., & Huang, D. (2018) · Horticulture Research · doi:10.1038/s41438-018-0050-1 · Cited by 108
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Shi, L., Holliday, A. E., Shi, H., Zhu, F., Ewing, M. A., Russell, D. H., & Clemmer, D. E. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505899g · Cited by 105
Zheng, X., Wojcik, R., Zhang, X., Ibrahim, Y., Burnum-Johnson, K., Orton, D., Monroe, M. E., Moore, R., Smith, R. D., & Baker, E. S. (2017) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-061516-045212 · Cited by 111
Beale, D. J., Jones, O. A. H., Karpe, A. V., Dayalan, S., Oh, D. Y., Kouremenos, K. A., Ahmed, W., & Palombo, E. A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010024 · Cited by 102
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Prasad, B., Achour, B., Artursson, P., Hop, C. E. C. A., Lai, Y., Smith, P. C., Barber, J., Wiśniewski, J. R., Spellman, D. S., Uchida, Y., et al. (2019) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.1537 · Cited by 101
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Kirk, A. T., Bohnhorst, A., Raddatz, C., Allers, M., & Zimmermann, S. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-01807-0 · Cited by 97
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Albanese, K. I., Barbe, S., Tagami, S., Woolfson, D. N., & Schiex, T. (2025) · Nature Reviews Methods Primers · doi:10.1038/s43586-025-00383-1 · Cited by 104
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Hofmann, J., Struwe, W. B., Scarff, C. A., Scrivens, J. H., Harvey, D. J., & Pagel, K. (2014) · Analytical Chemistry · doi:10.1021/ac5028353 · Cited by 94
Zheng, X., Zhang, X., Schocker, N. S., Renslow, R. S., Orton, D., Khamsi, J., Ashmus, R. A., de Almeida, I. C., Tang, K., Costello, C. E., et al. (2016) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-016-9866-4 · Cited by 99
Beck, M. W., Derrick, J. S., Kerr, R. A., Oh, S. B., Cho, W. J., Lee, S. J. C., Ji, Y., Han, J., Tehrani, Z. A., Suh, N., et al. (2016) · Nature Communications · doi:10.1038/ncomms13115 · Cited by 93
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Steckel, A., & Schlosser, G. (2019) · Molecules · doi:10.3390/molecules24030611 · Cited by 92
Mass spectrometry-enabled structural biology of membrane proteins
Calabrese, A. N., & Radford, S. E. (2018) · Methods · doi:10.1016/j.ymeth.2018.02.020 · Cited by 94
Conformational effects in protein electrospray‐ionization mass spectrometry
Li, J., Santambrogio, C., Brocca, S., Rossetti, G., Carloni, P., & Grandori, R. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21465 · Cited by 91
AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species
Ruggeri, F. S., Habchi, J., Cerreta, A., & Dietler, G. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160518141911 · Cited by 92
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Borges, R. M., Colby, S., Das, S., Edison, A. S., Fiehn, O., Kind, T., Lee, J., Merrill, A. T., Merz, K. M., Metz, T., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00901 · Cited by 93
A parallelized molecular collision cross section package with optimized accuracy and efficiency
Ieritano, C., Crouse, J., Campbell, J. L., & Hopkins, W. S. (2019) · The Analyst · doi:10.1039/c8an02150c · Cited by 90
McKenzie‐Coe, A., Montes, N., & Jones, L. M. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00432 · Cited by 87
Hernandez‐Alba, O., Isenberg, S. L., Steinmetz, V., Glish, G. L., & Maı̂tre, P. (2015) · The Journal of Physical Chemistry A · doi:10.1021/jp511975f · Cited by 86
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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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