Amphipathic agents are widely used in various fields including biomedical sciences. Micelle‐forming detergents are particularly useful for in vitro membrane‐protein characterization. As many conventional detergents are limited in their ability to stabilize membrane proteins, it is necessary to develop novel detergents to facilitate membrane‐protein research. In the current study, we developed novel trimaltoside detergents with an alkyl pendant‐bearing terphenyl unit as a hydrophobic group, designated terphenyl‐cored maltosides (TPMs). We found that the geometry of the detergent hydrophobic group substantially impacts detergent self‐assembly behavior, as well as detergent efficacy for membrane‐protein stabilization. TPM‐Vs, with a bent terphenyl group, were superior to the linear counterparts (TPM‐Ls) at stabilizing multiple membrane proteins. The favorable protein stabilization efficacy of these bent TPMs is likely associated with a binding mode with membrane proteins distinct from conventional detergents and facial amphiphiles. When compared to n‐dodecyl‐β‐d‐maltoside (DDM), most TPMs were superior or comparable to this gold standard detergent at stabilizing membrane proteins. Notably, TPM‐L3 was particularly effective at stabilizing the human β2 adrenergic receptor (β2AR), a G‐protein coupled receptor, and its complex with Gs protein. Thus, the current study not only provides novel detergent tools that are useful for membrane‐protein study, but also suggests a critical role for detergent hydrophobic group geometry in governing detergent efficacy.