Abstract
We have used native MS of membrane proteins liberated form micelles and native membranes to study protein lipid interactions. Using different Orbitrap MS platforms developed for membrane proteins we show that it is possible to distinguish lipids, cofactors and drugs while in direct contact with membrane protein targets.We also showed how drug binding mediates phosphorylation in a class A GPCR (P2Y1R) and that purification of three further class A GPCRs results in binding of specific lipids that mediate downstream coupling.The ability to detect binding which has both structural and functional effects for example on lipid flippase activity or G‐protein coupling, is a powerful and important attribute of the study of membrane proteins by mass spectrometry.Very recently we have added yet further insights by ejecting membrane protein directly from their native membrane environments. Recent results will be presented.Support or Funding InformationWellcome Trust Investigator AwardERC Advanced Grant MRC Programme Grant
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