Though ubiquitous in nature and relevant for ∼10% of all cellular proteins, posttranslational lipid modifications of proteins show an astonishing variety. Common motifs include myristoylations, palmitoylations, prenylations, and cholesterol modifications. All these structures show characteristic membrane properties. In recent years, we have studied a number of systems and elucidated the structure and dynamics of membrane embedded lipid modifications of proteins using solid-state NMR methods. In the presentation, a comparison of the membrane properties of several systems will be given: Farnesylated/hexadecylated Ras, myristoylated GCAP, myristoylated Src, and a transmembrane model peptide featuring lipid modifications of varying lengths between 2 and 16 carbons.