Lipid binding attenuates channel closure of the outer membrane protein OmpF
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DOI: 10.1073/pnas.1721152115
Abstract: Significance Outer-membrane porins are often considered as passive conduits of small molecules across lipid bilayers. Using native mass spectrometry experiments we identify a pH-sensitive lipid-binding mechanism of outer membrane porin F, which enables increased threading… read more here.
Keywords: mass spectrometry; lipid binding; attenuates channel; outer membrane ... See more keywords