Mass spectrometry: From plasma proteins to mitochondrial membranes
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Significance: Following initial discoveries of noncovalent associations surviving in the gas phase, only a few practitioners pursued this research area. Today scientists around the world are using these approaches to ascertain the heterogeneity and stoichiometry of proteins within complexes. Recent developments further highlight opportunities for studying the effects of protein glycosylation on antibody–antigen interactions and drug binding, as well as site-directed mutagenesis and posttranslational modification on membrane protein interfaces. As a result of many developments over the last two decades, mass spectrometry of protein complexes has exploded and is now undertaken not just in dedicated research laboratories in academia, but also in pharmaceutical and biotechnology companies. It is therefore timely to trace the history of these developments in this personal perspective.
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Many challenging analytes such as membrane proteins, intrinsically disordered proteins, highly dynamic or heterogeneous complexes, or very large systems such as intact virus capsids can all be investigated using native MS, as well as their associated proteoforms.
“By using appropriate sample preparation, ionisation conditions, and instrumentation, many challenging analytes such as membrane proteins,18,42 intrinsically disordered proteins,43 highly dynamic or heterogeneous complexes,19 or very large systems such as intact virus capsids44 can all be investigated using native MS, as well as their associated proteoforms.45”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [18]
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Membrane proteins bind lipids selectively to modulate their structure and function
Laganowsky, A. D., Reading, E., Allison, T. M., Ulmschneider, M. B., Degiacomi, M. T., Baldwin, A. J., & Robinson, C. V. (2014) · Nature · doi:10.1038/nature13419 · Cited by 786 · see citing works
Self-citationIon Mobility Measurements and their Applications to Clusters and Biomolecules
Clemmer, D. E., & Jarrold, M. F. (1997) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(199706)32:6 · Cited by 737 · see citing works
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 · see citing works
Evidence for Macromolecular Protein Rings in the Absence of Bulk Water
Ruotolo, B. T., Giles, K., Campuzano, I. D. G., Sandercock, A. M., Bateman, R. H., & Robinson, C. V. (2005) · Science · doi:10.1126/science.1120177 · Cited by 597 · see citing works
Self-citationDetection of Transient Protein Folding Populations by Mass Spectrometry
Miranker, A. D., Robinson, C. V., Radford, S. E., Aplin, R. T., & Dobson, C. M. (1993) · Science · doi:10.1126/science.8235611 · Cited by 546 · see citing works
Self-citationA Tandem Mass Spectrometer for Improved Transmission and Analysis of Large Macromolecular Assemblies
Sobott, F., Hernández, H., McCammon, M. G., Tito, M. A., & Robinson, C. V. (2002) · Analytical Chemistry · doi:10.1021/ac0110552 · Cited by 511 · see citing works
Self-citationThe role of interfacial lipids in stabilizing membrane protein oligomers
Gupta, K., Donlan, J. A. C., Hopper, J. T. S., Uzdavinys, P., Landreh, M., Struwe, W. B., Drew, D., Baldwin, A. J., Stansfeld, P. J., & Robinson, C. V. (2017) · Nature · doi:10.1038/nature20820 · Cited by 402 · see citing works
Self-citationHigh-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
Rose, R. J., Damoc, E., Denisov, E., Makarov, A., & Heck, A. J. R. (2012) · Nature Methods · doi:10.1038/nmeth.2208 · Cited by 392 · see citing works
Micelles Protect Membrane Complexes from Solution to Vacuum
Barrera, N. P., Bartolo, N. D. D., Booth, P. J., & Robinson, C. V. (2008) · Science · doi:10.1126/science.1159292 · Cited by 362 · see citing works
Self-citationStructure of the Rotor of the V-Type Na + -ATPase from Enterococcus hirae
Murata, T., Yamato, I., Kakinuma, Y., Leslie, A. G. W., & Walker, J. E. (2005) · Science · doi:10.1126/science.1110064 · Cited by 354 · see citing works
The rotary mechanism of ATP synthase
Stock, D., Gibbons, C., Aréchaga, I., Leslie, A. G. W., & Walker, J. E. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00147-0 · Cited by 325 · see citing works
MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis
Sham, L., Butler, E. K., Lebar, M. D., Kahne, D. E., Bernhardt, T. G., & Ruiz, N. (2014) · Science · doi:10.1126/science.1254522 · Cited by 322 · see citing works
Identification of FtsW as a transporter of lipid‐linked cell wall precursors across the membrane
Mohammadi, T., van Dam, V., Sijbrandi, R., Vernet, T., Zapun, A., Bouhss, A., Bruin, M. D.-D., Nguyen‐Distèche, M., KRUIJFF, B. D., & Breukink, E. J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.61 · Cited by 314 · see citing works
PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling
Yen, H.-Y., Hoi, K. K., Liko, I., Hedger, G., Horrell, M. R., Song, W., Wu, D., Heine, P., Warne, T., Lee, Y., et al. (2018) · Nature · doi:10.1038/s41586-018-0325-6 · Cited by 284 · see citing works
Self-citationZhou, M., Morgner, N., Barrera, N. P., Politis, A., Isaacson, S. C., Matak‐Vinković, D., Murata, T., Bernal, R. A., Stock, D., & Robinson, C. V. (2011) · Science · doi:10.1126/science.1210148 · Cited by 268 · see citing works
Self-citationHigh-resolution mass spectrometry of small molecules bound to membrane proteins
Gault, J., Donlan, J. A. C., Liko, I., Hopper, J. T. S., Gupta, K., Housden, N. G., Struwe, W. B., Marty, M. T., Mize, T. H., Bechara, C., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3771 · Cited by 237 · see citing works
Self-citationGas-phase folding and unfolding of cytochrome c cations.
Wood, T. D., Chorush, R. A., Wampler, F. M., Little, D. P., O’Connor, P. B., & McLafferty, F. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2451 · Cited by 232 · see citing works
Ruotolo, B. T., Hyung, S., Robinson, P. M., Giles, K., Bateman, R. H., & Robinson, C. V. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702161 · Cited by 229 · see citing works
Self-citationConformation of GroEL-bound α-lactalbumin probed by mass spectrometry
Robinson, C. V., Groß, M., Eyles, S. J., Ewbank, J. J., Mayhew, M., Hartl, F. U., Dobson, C. M., & Radford, S. E. (1994) · Nature · doi:10.1038/372646a0 · Cited by 199 · see citing works
Self-citationSubunit Exchange of Multimeric Protein Complexes
Sobott, F., Benesch, J. L. P., Vierling, E., & Robinson, C. V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206060200 · Cited by 199 · see citing works
Self-citationProtein assemblies ejected directly from native membranes yield complexes for mass spectrometry
Chorev, D. S., Baker, L. A., Wu, D., Beilsten-Edmands, V., Rouse, S. L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., et al. (2018) · Science · doi:10.1126/science.aau0976 · Cited by 191 · see citing works
Self-citationDetection of the Intact GroEL Chaperonin Assembly by Mass Spectrometry
Rostom, A. A., & Robinson, C. V. (1999) · Journal of the American Chemical Society · doi:10.1021/ja990238r · Cited by 179 · see citing works
Self-citationMass spectrometry of membrane transporters reveals subunit stoichiometry and interactions
Barrera, N. P., Isaacson, S. C., Zhou, M., Bavro, V. N., Welch, A., Schaedler, T. A., Seeger, M., Miguel, R., Korkhov, V. M., van Veen, H. V., et al. (2009) · Nature Methods · doi:10.1038/nmeth.1347 · Cited by 175 · see citing works
Self-citationMarcoux, J., Wang, S. C., Politis, A., Reading, E., Ma, J., Biggin, P. C., Zhou, M., Tao, H., Zhang, Q., Chang, G. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303888110 · Cited by 170 · see citing works
Self-citationThermal Dissociation of Multimeric Protein Complexes by Using Nanoelectrospray Mass Spectrometry
Benesch, J. L. P., Sobott, F., & Robinson, C. V. (2003) · Analytical Chemistry · doi:10.1021/ac034132x · Cited by 169 · see citing works
Self-citationMorgner, N., & Robinson, C. V. (2012) · Analytical Chemistry · doi:10.1021/ac300056a · Cited by 152 · see citing works
Self-citationIwata, M., Imamura, H., Stambouli, E., Ikeda, C., Tamakoshi, M., Nagata, K., Makyio, H., Hankamer, B. D., Barber, J., Yoshida, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305165101 · Cited by 139 · see citing works
A subset of annular lipids is linked to the flippase activity of an ABC transporter
Bechara, C., Noll, A., Morgner, N., Degiacomi, M. T., Tampé, R., & Robinson, C. V. (2015) · Nature Chemistry · doi:10.1038/nchem.2172 · Cited by 124 · see citing works
Self-citationIntrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF
Housden, N. G., Hopper, J. T. S., Lukoyanova, N., Rodríguez‐Larrea, D., Wojdyla, J. A., Klein, A., Kaminska, R., Bayley, H., Saibil, H. R., Robinson, C. V., et al. (2013) · Science · doi:10.1126/science.1237864 · Cited by 120 · see citing works
Self-citationImaging proteins at the single-molecule level
Longchamp, J.-N., Rauschenbach, S., Abb, S., Escher, C., Latychevskaia, T., Kern, K., & Fink, H.-W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614519114 · Cited by 119 · see citing works
Dynamic tuneable G protein-coupled receptor monomer-dimer populations
Dijkman, P. M., Castell, O. K., Goddard, A. D., Muñoz-García, J. C., de Graaf, C., Wallace, M. I., & Watts, A. G. (2018) · Nature Communications · doi:10.1038/s41467-018-03727-6 · Cited by 116 · see citing works
Identifying key membrane protein lipid interactions using mass spectrometry
Gupta, K., Li, J., Liko, I., Gault, J., Bechara, C., Wu, D., Hopper, J. T. S., Giles, K., Benesch, J. L. P., & Robinson, C. V. (2018) · Nature Protocols · doi:10.1038/nprot.2018.014 · Cited by 112 · see citing works
Self-citationRemoval of detergents from protein digests for mass spectrometry analysis
Yeung, Y.-G., Nieves, E., Angeletti, R. H., & Stanley, E. R. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.07.034 · Cited by 103 · see citing works
Fändrich, M., Tito, M. A., Leroux, M. R., Rostom, A. A., Hartl, F. U., Dobson, C. M., & Robinson, C. V. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240326597 · Cited by 100 · see citing works
Self-citationInterrogating Membrane Protein Conformational Dynamics within Native Lipid Compositions
Reading, E., Hall, Z., Martens, C., Haghighi, T., Findlay, H. E., Ahdash, Z., Politis, A., & Booth, P. J. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709657 · Cited by 100 · see citing works
Lipid Flippases for Bacterial Peptidoglycan Biosynthesis
Ruiz, N. (2015) · Lipid Insights · doi:10.4137/lpi.s31783 · Cited by 98 · see citing works
Reading, E., Walton, T. A., Liko, I., Marty, M. T., Laganowsky, A. D., Rees, D. C., & Robinson, C. V. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.04.016 · Cited by 85 · see citing works
Self-citationLarge-scale production and protein engineering of G protein-coupled receptors for structural studies
Milić, D., & Veprintsev, D. B. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00066 · Cited by 84 · see citing works
Bernal, R. A., & Stock, D. (2004) · Structure · doi:10.1016/j.str.2004.07.017 · Cited by 84 · see citing works
Toei, M., Gerle, C., Nakano, M., Tani, K., Gyobu, N., Tamakoshi, M., Sone, N., Yoshida, M., Fujiyoshi, Y., Mitsuoka, K., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706914105 · Cited by 82 · see citing works
Direct observation of the influence of cardiolipin and antibiotics on lipid II binding to MurJ
Bolla, J. R., Sauer, J. B., Wu, D., Mehmood, S., Allison, T. M., & Robinson, C. V. (2018) · Nature Chemistry · doi:10.1038/nchem.2919 · Cited by 77 · see citing works
Self-citationMass-Selective Soft-Landing of Protein Assemblies with Controlled Landing Energies
Mikhailov, V. A., Mize, T. H., Benesch, J. L. P., & Robinson, C. V. (2014) · Analytical Chemistry · doi:10.1021/ac5018327 · Cited by 71 · see citing works
Self-citationBenesch, J. L. P., Ruotolo, B. T., Simmons, D. A., Barrera, N. P., Morgner, N., Wang, L., Saibil, H. R., & Robinson, C. V. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.03.004 · Cited by 69 · see citing works
Self-citationLigand binding to a G protein–coupled receptor captured in a mass spectrometer
Yen, H., Hopper, J. T. S., Liko, I., Allison, T. M., Zhu, Y., Wang, D., Stegmann, M., Mohammed, S., Wu, B., & Robinson, C. V. (2017) · Science Advances · doi:10.1126/sciadv.1701016 · Cited by 67 · see citing works
Self-citationDrug Binding Revealed by Tandem Mass Spectrometry of a Protein−Micelle Complex
Ilag, L. L., Ubarretxena‐Belandia, I., Tate, C. G., & Robinson, C. V. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0450307 · Cited by 65 · see citing works
Self-citationRostom, A. A., Sunde, M., Richardson, S. J., Schreiber, G., Jarvis, S., Bateman, R. H., Dobson, C. M., & Robinson, C. V. (1998) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(1998)33:2+ · Cited by 63 · see citing works
Self-citationAtomic-level analysis of membrane-protein structure
Hendrickson, W. A. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3215 · Cited by 57 · see citing works
Hellwig, N., Peetz, O., Ahdash, Z., Tascón, I., Booth, P. J., Mikušević, V., Diskowski, M., Politis, A., Hellmich, Y., Hänelt, I., et al. (2018) · Chemical Communications · doi:10.1039/c8cc06284f · Cited by 55 · see citing works
Esteban, O., Bernal, R. A., Donohoe, M., Videler, H., Sharon, M., Robinson, C. V., & Stock, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704941200 · Cited by 51 · see citing works
Self-citationLipid binding attenuates channel closure of the outer membrane protein OmpF
Liko, I., Degiacomi, M. T., Lee, S., Newport, T. D., Gault, J., Reading, E., Hopper, J. T. S., Housden, N. G., White, P. C., Colledge, M., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721152115 · Cited by 49 · see citing works
Self-citationLengqvist, J., Svensson, R., Evergren, E., Morgenstern, R., & Griffiths, W. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310958200 · Cited by 48 · see citing works
Landreh, M., Costeira-Paulo, J., Gault, J., Marklund, E. G., & Robinson, C. V. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00922 · Cited by 45 · see citing works
Self-citationMass spectrometry across the sciences
McLafferty, F. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800784105 · Cited by 32 · see citing works
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Konermann, L., Metwally, H., Duez, Q., & Peters, I. (2019) · The Analyst · doi:10.1039/c9an01201j · Cited by 76 · see citing works
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Hassan, M. M., & Olaoye, O. O. (2020) · Molecules · doi:10.3390/molecules25102285 · Cited by 54 · see citing works
Xu, T., Wang, Q., Wang, Q., & Sun, L. (2024) · Analytical Methods · doi:10.1039/d4ay00651h · Cited by 53 · see citing works
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Grime, G. W., Zeldin, O. B., Snell, M. E., Lowe, E. D., Hunt, J. F., Montelione, G. T., Tong, L., Snell, E. H., & Garman, E. F. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b09186 · Cited by 41 · see citing works
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Li, L., Zhang, Y., Lv, Y., Qu, F., & Ma, Q. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117424 · Cited by 6 · see citing works
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Villacob, R. A., Egbejiogu, B. C., Feizi, N., Hogan, C., Murray, K. K., & Solouki, T. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00184 · Cited by 5 · see citing works
A chemometric-assisted voltammetric analysis of free and Zn(II)-loaded metallothionein-3 states
Peris‐Díaz, M. D., Richtera, L., Zítka, O., Krężel, A., & Adam, V. (2020) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2020.107501 · Cited by 5 · see citing works
Villacob, R. A., Feizi, N., Beno, S. C., & Solouki, T. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00261 · Cited by 4 · see citing works
Donald, L. J., Spearman, M. A., Mishra, N., Komatsu, E., Butler, M., & Perreault, H. (2020) · Molecular Omics · doi:10.1039/c9mo00168a · Cited by 4 · see citing works
Maciel, E. V. S., Eisert, J., Hake, C., Schießer, A., & Lermyte, F. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c05700 · Cited by 3 · see citing works
Escobar, E. E., Yang, W., Lanzillotti, M. B., Juetten, K. J., Shields, S., Siegel, D. R., Zhang, Y., & Brodbelt, J. S. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00098 · Cited by 3 · see citing works
Advanced Technologies for Protein Complex Production and Characterization
Vega, M. C., & Fernández, F. J. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-52193-5 · Cited by 3 · see citing works
Whitelegge, J. P. (2020) · Proteomes · doi:10.3390/proteomes8010005 · Cited by 2 · see citing works
Jia, M., Sen, S., Wachnowsky, C., Fidai, I., Cowan, J. A., & Wysocki, V. H. (2020) · Angewandte Chemie · doi:10.1002/ange.201915615 · Cited by 1 · see citing works
Erba, E. B., & Pastore, A. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-52193-5_8 · Cited by 1 · see citing works
Structural Characterization of Protein Complexes Using Native Mass Spectrometry
Saikusa, K. (2024) · Journal of the Mass Spectrometry Society of Japan · doi:10.5702/massspec.24-132 · Cited by 1 · see citing works
Profile of Dame Carol Robinson
Viegas, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903862116
Screening and Characterizing of GPCR –Ligand Interactions with Mass Spectrometry‐Based Technologies
Qin, S., Lu, Y., & Shui, W. (2022) · doi:10.1002/9781119564782.ch22
- Authors
- Robinson, C. V.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Robinson, Carol V.
- ORCID
- Robinson, Carol V.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-02-04
- Volume
- 116
- Issue
- 8
- Pages
- 2814-2820
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6386728
- OpenAlex
- W2911977783
- Cited by
- 53
- References
- 53
- Citations by year
- 2026: 1 · 2024: 10 · 2023: 4 · 2022: 8 · 2021: 9 · 2020: 17 · 2019: 4
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust (104633/Z/14/Z)
- Medical Research Council (MR/N020413/1)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- plasma proteins, membrane protein assembly, mitochondrial membrane, ion mobility, soft landing, detergent micelles, protein-lipid interactions, G protein-coupled receptors, protein oligomerization, subunit stoichiometry
- MeSH terms
- Blood Proteins, Membrane Proteins, Mass Spectrometry, Mitochondrial Membranes, Biophysical Phenomena
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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