The DOI matches its Crossref record.
Collision Cross Sections of Proteins and Their Complexes: A Calibration Framework and Database for Gas-Phase Structural Biology
Abstract
Collision cross sections in both helium and nitrogen gases were measured directly using a drift cell with RF ion confinement inserted within a quadrupole/ion mobility/time-of-flight hybrid mass spectrometer (Waters Synapt HDMS, Manchester, U.K.). Collision cross sections for a large set of denatured peptide, denatured protein, native-like protein, and native-like protein complex ions are reported here, forming a database of collision cross sections that spans over 2 orders of magnitude. The average effective density of the native-like ions is 0.6 g cm(-3), which is significantly lower than that for the solvent-excluded regions of proteins and suggests that these ions can retain significant memory of their solution-phase structures rather than collapse to globular structures. Because the measurements are acquired using an instrument that mimics the geometry of the commercial Synapt HDMS instrument, this database enables the determination of highly accurate collision cross sections from traveling-wave ion mobility data through the use of calibration standards with similar masses and mobilities. Errors in traveling-wave collision cross sections determined for native-like protein complexes calibrated using other native-like protein complexes are significantly less than those calibrated using denatured proteins. This database indicates that collision cross sections in both helium and nitrogen gases can be well-correlated for larger biomolecular ions, but non-correlated differences for smaller ions can be more significant. These results enable the generation of more accurate three-dimensional models of protein and other biomolecular complexes using gas-phase structural biology techniques.
Overview
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
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
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
Self-citationLanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E. (2014) · Nature Chemistry · doi:10.1038/nchem.1889 · Cited by 901
Membrane proteins bind lipids selectively to modulate their structure and function
Laganowsky, A., 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 781
Self-citationRecommendations for reporting ion mobility Mass Spectrometry measurements
Gabelica, V., Shvartsburg, A. A., Afonso, C., Barran, P., Benesch, J. L. P., Bleiholder, C., Bowers, M. T., Bilbao, A., Bush, M. F., Campbell, J. L., et al. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21585 · Cited by 493
Self-citationFundamentals of ion mobility spectrometry
Gabelica, V., & Marklund, E. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.10.022 · Cited by 440
Campuzano, I., Bush, M. F., Robinson, C. V., Beaumont, C., Richardson, K., Kim, H., & Kim, H. I. (2012) · Analytical Chemistry · doi:10.1021/ac202625t · Cited by 383
Self-citationTrapped 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 308
Collision Cross Sections for Structural Proteomics
Marklund, E. G., Degiacomi, M. T., Robinson, C. V., Baldwin, A. J., & Benesch, J. L. P. (2015) · Structure · doi:10.1016/j.str.2015.02.010 · Cited by 270
Self-citationHall, 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
Self-citationSusa, A. C., Xia, Z., & Williams, E. R. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04897 · Cited by 167
Probing the biophysical interplay between a viral genome and its capsid
Snijder, J., Uetrecht, C., Rose, R. J., Sanchez-Eugenia, R., Marti, G. A., Agirre, J., Guérin, D. M. A., Wuite, G. J. L., Heck, A. J. R., & Roos, W. H. (2013) · Nature Chemistry · doi:10.1038/nchem.1627 · Cited by 127
Zhou, M., Dagan, S., & Wysocki, V. H. (2013) · The Analyst · doi:10.1039/c2an36525a · Cited by 92
Wongkongkathep, P., Han, J. Y., Choi, T. S., Yin, S., Kim, H. I., & Loo, J. A. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2002-2 · Cited by 71
Vimer, S., Ben-Nissan, G., Morgenstern, D., Kumar-Deshmukh, F., Polkinghorn, C., Quintyn, R. S., Vasil’ev, Y. V., Beckman, J. S., Elad, N., Wysocki, V. H., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00080 · Cited by 63
Ion mobility in the pharmaceutical industry: an established biophysical technique or still niche?
Campuzano, I. D., & Lippens, J. L. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.11.008 · Cited by 42
Mikhailov, V. A., Griffiths, R. L., & Cooper, H. J. (2017) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.09.011 · Cited by 41
Allison, T. M., Barran, P., Cianférani, S., Degiacomi, M. T., Gabelica, V., Grandori, R., Marklund, E. G., Menneteau, T., Migas, L. G., Politis, A., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05791 · Cited by 38
Recent technological developments for native mass spectrometry
Webb, I. K. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140732 · Cited by 29
Shepherd, D. A., Holmes, K., Rowlands, D. J., Stonehouse, N. J., & Ashcroft, A. E. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.07.028 · Cited by 25
Metadata
- Authors
- Bush, M. F., Hall, Z., Giles, K., Hoyes, J., Robinson, C. V., & Ruotolo, B. T.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-10-27
- Volume
- 82
- Issue
- 22
- Pages
- 9557-9565
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2317233863
- Cited by
- 796
- References
- 0
- FWCI
- 14.92
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
