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Journal article

Low charge and reduced mobility of membrane protein complexes has implications for calibration of collision cross section measurements

Abstract:

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
Version:
Accepted manuscript

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Publisher copy:
10.1021/acs.analchem.6b00691

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
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Funding agency for:
Landreh, M
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Funding agency for:
Benesch, JL
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Funding agency for:
Robinson, CV
More from this funder
Funding agency for:
Robinson, CV
Publisher:
American Chemical Society Publisher's website
Journal:
Analytical Chemistry Journal website
Volume:
88
Issue:
11
Pages:
5879–5884
Publication date:
2016-05-06
DOI:
EISSN:
1520-6882
ISSN:
0003-2700
URN:
uuid:297f1416-2458-4b49-acd2-a85bee393a86
Source identifiers:
623124
Local pid:
pubs:623124
Paper number:
11
Language:
English

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