The study of membrane proteins is undergoing a golden era, and we are gaining unprecedented knowledge on how this key group of proteins works. However, we still have only a basic understanding of how the chemical composition and the physical properties of lipid bilayers control the activity of membrane proteins. Single-molecule (SM) fluorescence methods can resolve sample heterogeneity, allowing to discriminate between the different molecular populations that biological systems often adopt. This short review highlights relevant examples of how SM fluorescence methodologies can illuminate the different ways in which lipids regulate the activity of membrane proteins. These studies are not limited to lipid molecules acting as ligands, but also consider how the physical properties of the bilayer can be determining factors on how membrane proteins function.
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Cardiff Univ, Coll Biomed & Life Sci, Sch Pharm & Pharmaceut Sci, King Edward VII Ave, Cardiff CF10 3NB, S Glam, WalesCardiff Univ, Coll Biomed & Life Sci, Sch Pharm & Pharmaceut Sci, King Edward VII Ave, Cardiff CF10 3NB, S Glam, Wales
Castell, Oliver K.
Dijkman, Patricia M.
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Max Planck Inst Biophys, Max von Laue Str 3, D-60438 Frankfurt, GermanyCardiff Univ, Coll Biomed & Life Sci, Sch Pharm & Pharmaceut Sci, King Edward VII Ave, Cardiff CF10 3NB, S Glam, Wales
Dijkman, Patricia M.
Wiseman, Daniel N.
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Aston Univ, Sch Life & Hlth Sci, Birmingham B4 7ET, W Midlands, EnglandCardiff Univ, Coll Biomed & Life Sci, Sch Pharm & Pharmaceut Sci, King Edward VII Ave, Cardiff CF10 3NB, S Glam, Wales
Wiseman, Daniel N.
Goddard, Alan D.
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Aston Univ, Sch Life & Hlth Sci, Birmingham B4 7ET, W Midlands, EnglandCardiff Univ, Coll Biomed & Life Sci, Sch Pharm & Pharmaceut Sci, King Edward VII Ave, Cardiff CF10 3NB, S Glam, Wales