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Journal article

Lipid binding attenuates channel closure of the outer membrane protein OmpF

Abstract:

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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Publisher copy:
10.1073/pnas.1721152115

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
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Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences Journal website
Volume:
115
Issue:
26
Pages:
6691–6696
Publication date:
2018-06-11
Acceptance date:
2018-04-30
DOI:
ISSN:
e1091-6490 and 0027-8424
Pmid:
29891712
Source identifiers:
857132
Language:
English
Keywords:
Pubs id:
pubs:857132
UUID:
uuid:2bd5ba93-8450-4b39-9fc1-feefe5a1ae70
Local pid:
pubs:857132
Deposit date:
2018-07-10

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