Cells and organelles are enclosed by lipid bilayers that separate them from their external environment. Embedded in these membranes are particular proteins that span the full width of the bilayer and mediate communication between the two sides. These membrane proteins carry out a multitude of tasks and adopt different architectures, ranging from single transmembrane‐spanning domains to large multimeric assemblies. Although membrane proteins constitute more than 30% of known proteins, they represent less than 1% of the high‐resolution protein structures deposited in the Protein Data Bank. Their hydrophobicity and their dependence on lipids render them difficult to crystallize and to purify in a soluble form. Recent developments performed in solid‐state NMR spectroscopy offer unique opportunities to address such systems on the atomic level in their native environment. Indeed, membrane proteins have been the subject of solid‐state NMR for more than three decades, and pioneering studies on bacteriorhodopsin [