Journal article
Low charge and reduced mobility of membrane protein complexes has implications for calibration of collision cross section measurements
- Abstract:
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Ion mobility mass spectrometry of integral membrane proteins provides valuable insights into their architecture and stability. Here we show that, due to their lower charge, the average mobility of native-like membrane protein ions is approximately 30% lower than that of soluble proteins of similar mass. This has implications for drift time measurements, made on traveling wave ion mobility mass spectrometers, which have to be calibrated to extract collision cross sections (Ω). Common calibrati...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Accepted manuscript, tiff, 4.0MB)
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(Accepted manuscript, pdf, 641.1KB)
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(Accepted manuscript, pdf, 217.5KB)
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- Publisher copy:
- 10.1021/acs.analchem.6b00691
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Authors
Funding
+ St. Cross College, University of Oxford
More from this funder
Funding agency for:
Landreh, M
Grant:
Junior Research Fellowship
+ Marie Curie
More from this funder
Funding agency for:
Landreh, M
Grant:
Junior Research Fellowship
+ European Research Council
More from this funder
Funding agency for:
Robinson, C
Grant:
Research Professorship
+ Royal Society
More from this funder
Funding agency for:
Benesch, J
Grant:
University Research Fellow
Bibliographic Details
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Analytical Chemistry Journal website
- Volume:
- 88
- Issue:
- 11
- Pages:
- 5879–5884
- Publication date:
- 2016-05-06
- Acceptance date:
- 2016-05-06
- DOI:
- EISSN:
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1520-6882
- ISSN:
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0003-2700
- Source identifiers:
-
623124
Item Description
- Language:
- English
- Pubs id:
-
pubs:623124
- UUID:
-
uuid:297f1416-2458-4b49-acd2-a85bee393a86
- Local pid:
- pubs:623124
- Deposit date:
- 2016-05-23
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2016
- Notes:
- Copyright © 2016 American Chemical Society. This is the accepted manuscript version of the article. The final version is available online from the American Chemical Society at: [10.1021/acs.analchem.6b00691]
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