High-resolution mass spectrometry of small molecules bound to membrane proteins.
Joseph GaultJoseph A C DonlanIdlir LikoJonathan T S HopperKallol GuptaNicholas G HousdenWeston B StruweMichael T MartyTodd MizeCherine BecharaYa ZhuBeili WuColin KleanthousMikhail BelovEugen DamocAlexander MakarovCarol V RobinsonPublished in: Nature methods (2016)
Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry-based method for analyzing intact membrane protein-ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length.
Keyphrases
- high resolution mass spectrometry
- liquid chromatography
- mass spectrometry
- high resolution
- small molecule
- tandem mass spectrometry
- gas chromatography
- ultra high performance liquid chromatography
- high performance liquid chromatography
- simultaneous determination
- dna binding
- fatty acid
- solid phase extraction
- capillary electrophoresis
- genome wide
- binding protein
- high throughput
- single cell
- protein protein
- gene expression