Revealing the Quaternary Structure of a Heterogeneous Noncovalent Protein Complex through Surface-Induced Dissociation
Open accessAbstract
As scientists begin to appreciate the extent to which quaternary structure facilitates protein function, determination of the subunit arrangement within noncovalent protein complexes is increasingly important. While native mass spectrometry shows promise for the study of noncovalent complexes, few developments have been made toward the determination of subunit architecture, and no mass spectrometry activation method yields complete topology information. Here, we illustrate the surface-induced dissociation of a heterohexamer, toyocamycin nitrile hydratase, directly into its constituent trimers. We propose that the single-step nature of this activation in combination with high energy deposition allows for dissociation prior to significant unfolding or other large-scale rearrangement. This method can potentially allow for dissociation of a protein complex into subcomplexes, facilitating the mapping of subunit contacts and thus determination of quaternary structure of protein complexes.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Native MS provides information on protein complex subunit stoichiometry, metal binding, protein interaction partners, and lipid binding.
“Valuable information regarding protein complex subunit stoichiometry [42], metal-binding [43,44], protein interaction partners [45], and lipid binding [46] can be achieved using native MS.”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [42]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
van den Heuvel, R. H. H., van Duijn, E., Mazon, H., Synowsky, S. A., Lorenzen, K., Versluis, C., Brouns, S. J. J., Langridge, D., John van der, O. O. S. T., Hoyes, J. B., et al. (2006) · Analytical Chemistry · doi:10.1021/ac061039a · Cited by 252 · see citing works
Aspects of native proteins are retained in vacuum
Ruotolo, B. T., & Robinson, C. V. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.08.020 · Cited by 237 · see citing works
Tandem Mass Spectrometry Reveals the Quaternary Organization of Macromolecular Assemblies
Benesch, J. L. P., Aquilina, J. A., Ruotolo, B. T., Sobott, F., & Robinson, C. V. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.04.006 · Cited by 223 · see citing works
Collisions of ions with surfaces at chemically relevant energies: Instrumentation and phenomena
Grill, V., Shen, J., Evans, C., et al. (2001) · Review of Scientific Instruments · doi:10.1063/1.1382641 · Cited by 218 · see citing works
Collisional activation of protein complexes: Picking up the pieces
Benesch, J. L. P. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.11.014 · Cited by 195 · see citing works
Alternate Dissociation Pathways Identified in Charge-Reduced Protein Complex Ions
Pagel, K., Hyung, S., Ruotolo, B. T., & Robinson, C. V. (2010) · Analytical Chemistry · doi:10.1021/ac101121r · Cited by 157 · see citing works
Symmetrical Modularity of the COP9 Signalosome Complex Suggests its Multifunctionality
Sharon, M., Mao, H., Erba, E. B., Stephens, E., Zheng, N., & Robinson, C. V. (2009) · Structure · doi:10.1016/j.str.2008.10.012 · Cited by 155 · 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
How far can we go with structural mass spectrometry of protein complexes?
Sharon, M. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2009.12.017 · Cited by 93 · see citing works
McCarty, R. M., & Bandarian, V. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.07.012 · Cited by 89 · see citing works
Self-citationWysocki, V. H., Jones, C. M., Galhena, A. S., & Blackwell, A. E. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.04.026 · Cited by 86 · see citing works
Self-citationShen, H., & Chou, K. (2009) · Journal of Proteome Research · doi:10.1021/pr800957q · Cited by 85 · see citing works
Symmetrical gas-phase dissociation of noncovalent protein complexes via surface collisions.
Jones, C. M., Beardsley, R. L., Galhena, A. S., Dagan, S., Cheng, G., & Wysocki, V. (2006) · Journal of the American Chemical Society · doi:10.1021/ja064586m · Cited by 81 · see citing works
Self-citationNoncovalent Protein Tetramers and Pentamers with “n” Charges Yield Monomers with n/4 and n/5 Charges
Beardsley, R. L., Jones, C. M., Galhena, A. S., & Wysocki, V. H. (2009) · Analytical Chemistry · doi:10.1021/ac801883k · Cited by 76 · see citing works
Self-citationEnergy transfer in collisions of peptide ions with surfaces
Laskin, J., & Futrell, J. H. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1589739 · Cited by 72 · see citing works
Erba, E. B., Ruotolo, B. T., Barsky, D., & Robinson, C. V. (2010) · Analytical Chemistry · doi:10.1021/ac101778e · Cited by 71 · see citing works
Galhena, A. S., Dagan, S., Jones, C. M., Beardsley, R. L., & Wysocki, V. H. (2008) · Analytical Chemistry · doi:10.1021/ac701782q · Cited by 64 · see citing works
Self-citationSchoeller, D. A., Colligan, A. S., Shriver, T. C., Avak, H., & Bartok, C. (2000) · Journal of Mass Spectrometry · doi:10.1002/1096-9888(200009)35:9 · Cited by 54 · see citing works
Aquilina, J. A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22259 · Cited by 34 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Hall, Z., Politis, A., Bush, M. F., Smith, L. J., & Robinson, C. V. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2096859 · Cited by 267 · see citing works
Belov, M. E., Damoc, E., Denisov, E., Compton, P. D., Horning, S., Makarov, A. A., & Kelleher, N. L. (2013) · Analytical Chemistry · doi:10.1021/ac4029328 · Cited by 175 · see citing works
Top-down proteomics: challenges, innovations, and applications in basic and clinical research
Brown, K. A., Melby, J. A., Roberts, D. S., & Ge, Y. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1855982 · Cited by 152 · see citing works
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 · see citing works
Zhou, M., Dagan, S., & Wysocki, V. H. (2013) · The Analyst · doi:10.1039/c2an36525a · Cited by 92 · see citing works
Self-citationBelov, A. M., Viner, R., Santos, M. R., Horn, D. M., Bern, M., Karger, B. L., & Ivanov, A. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1781-1 · Cited by 97 · see citing works
- Authors
- Blackwell, A. E., Dodds, E. D., Bandarian, V., & Wysocki, V. H.
- Affiliations
- University of Arizona (US)
- Corresponding author
- Wysocki, Vicki H.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-03-21
- Volume
- 83
- Issue
- 8
- Pages
- 2862-2865
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC3343771
- OpenAlex
- W2045907498
- Cited by
- 84
- References
- 20
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 5 · 2019: 4 · 2018: 2 · 2017: 5 · 2016: 8 · 2015: 12 · 2014: 8 · 2013: 9 · 2012: 11
- FWCI
- 4.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM072623)
- 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 › Protein Structure and Dynamics
- Keywords
- quaternary structure, noncovalent protein complexes, surface-induced dissociation, heterohexamer, trimers, protein complex dissociation
- MeSH terms
- Hydro-Lyases, Models, Molecular, Surface Properties, Toyocamycin, Protein Structure, Quaternary, Protein Subunits
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
