Journal article
Lipid binding attenuates channel closure of the outer membrane protein OmpF
- Abstract:
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Strong interactions between lipids and proteins occur primarily through association of charged headgroups and amino acid side chains, rendering the protonation status of both partners important. Here we use native mass spectrometry to explore lipid binding as a function of charge of the outer membrane porin F (OmpF). We find that binding of anionic phosphatidylglycerol (POPG) or zwitterionic phosphatidylcholine (POPC) to OmpF is sensitive to electrospray polarity while the effects of charge a...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 1.3MB, Terms of use)
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- Publisher copy:
- 10.1073/pnas.1721152115
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Funding
Bibliographic Details
- Publisher:
- National Academy of Sciences
- Journal:
- Proceedings of the National Academy of Sciences More from this journal
- Volume:
- 115
- Issue:
- 26
- Pages:
- 6691–6696
- Publication date:
- 2018-06-11
- Acceptance date:
- 2018-04-30
- DOI:
- ISSN:
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e1091-6490 and 0027-8424
- Pmid:
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29891712
Item Description
- Language:
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English
- Keywords:
- Pubs id:
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pubs:857132
- UUID:
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uuid:2bd5ba93-8450-4b39-9fc1-feefe5a1ae70
- Local pid:
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pubs:857132
- Source identifiers:
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857132
- Deposit date:
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2018-07-10
Terms of use
- Copyright holder:
- Liko et al
- Copyright date:
- 2018
- Notes:
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© The Authors 2018. Published by PNAS.
This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
- Licence:
- CC Attribution (CC BY)
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