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Significance Biological membranes are semipermeable barriers that are composed primarily of phospholipid bilayers or monolayers and proteins. Proteins embedded within membranes are extremely diverse in structure and function. Some membrane-integrated proteins do not fully span phospholipid bilayers but play key roles in organizing membrane surfaces. How these monolayer-integrated proteins interact with membranes has not been systematically investigated, primarily because they are very difficult to distinguish from the far more common class of proteins that fully traverse the phospholipid bilayer. We describe an approach to systematically identify monolayer-integrated proteins and demonstrate that interfacial α-helices are a structural motif that directs membrane integration for this important class of membrane protein.

Proteomic analysis of monolayer-integrated proteins on lipid droplets identifies amphipathic interfacial α-helical membrane anchors