Mass spectrometry has long been the tool of choice for the analytical chemist for characterising small molecules. Recent developments however have made it possible to study proteins from their native states and have led to breakthroughs in projecting membrane protein complexes from solution into the gas phase. With these developments came the realization that the lipid environment is crucial for maintaining the structure of membrane proteins even in the gas phase. Today mass spectrometry, is emerging as one of the most exciting ways to monitor different modes of lipid binding to membrane protein complexes. Initial studies monitored the addition of lipids and deduced the kinetic and thermodynamic effects of lipid binding to proteins. Recently however, we have focused on identifying lipids already present, explicitly in plugs, annular rings or cavities. Lipids that bind within these orifices to membrane proteins will have higher residence times than those in the bulk lipid bilayer and consequently can be quantified and characterized by mass spectrometry. In special cases, lipids identified within cavities have been proposed as substrates following activity assays. Alternatively, a gas phase unfolding protocol can be used to distinguish lipids that are important for stability. In this lecture I will provide an overview of recent advances in mass spectrometry, with a particular focus on the distinction of the various modes of lipid binding, their implications for structure and function, as well as new directions that lie ahead. <br/>

Mass spectrometry of membrane proteins - the lipid connection

253rd National Meeting (2017)

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