Ontology highlight
ABSTRACT:
SUBMITTER: Cong X
PROVIDER: S-EPMC5736629 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Nature communications 20171219 1
The diverse lipid environment of the biological membrane can modulate the structure and function of membrane proteins. However, little is known about the role that lipids play in modulating protein-protein interactions. Here we employed native mass spectrometry (MS) to determine how individual lipid-binding events to the ammonia channel (AmtB) modulate its interaction with the regulatory protein, GlnK. The thermodynamic signature of AmtB-GlnK in the absence of lipids indicates conformational dyn ...[more]