AI Article Synopsis
- Recent advances in native mass spectrometry and ion mobility techniques now allow researchers to analyze membrane protein complexes in their gas-phase.
- This review highlights experimental methods used to study the dynamic structures of these proteins, including how lipid binding affects them and how they change during processes like ion channel gating.
- The research focuses on optimizing the reconstitution of membrane proteins for analysis, exploring compatibility with various lipid and detergent systems, and establishing parameters for examining their structural characteristics and interactions.
Article Abstract
Recent developments in native mass spectrometry and ion mobility have made it possible to analyze the composition and structure of membrane protein complexes in the gas-phase. In this short review we discuss the experimental strategies that allow to elucidate aspects of the dynamic structure of these important drug targets, such as the structural effects of lipid binding or detection of co-populated conformational and assembly states during gating on an ion channel. As native mass spectrometry relies on nano-electrospray of natively reconstituted proteins, a number of commonly used lipid- and detergent-based reconstitution systems have been evaluated for their compatibility with this approach, and parameters for the release of intact, native-like folded membrane proteins studied in the gas-phase. The strategy thus developed can be employed for the investigation of the subunit composition and stoichiometry, oligomeric state, conformational changes, and lipid and drug binding of integral membrane proteins.
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