10.1021/ja051275n.s001 Evan Kelly Evan Kelly Gilbert G. Privé Gilbert G. Privé D. Peter Tieleman D. Peter Tieleman Molecular Models of Lipopeptide Detergents:  Large Coiled-Coils with Hydrocarbon Interiors American Chemical Society 2005 octameric micelles form orientation detergent helix acyl chains acyl chain lengths model 2005-10-05 00:00:00 Journal contribution https://acs.figshare.com/articles/journal_contribution/Molecular_Models_of_Lipopeptide_Detergents_Large_Coiled_Coils_with_Hydrocarbon_Interiors/3264427 We have constructed molecular models of octameric micelles formed by a recently developed lipopeptide detergent consisting of a single amphipathic α-helix coupled to two acyl chains at either end of the helix. The models explain the experimentally observed aggregation behavior of peptides with different acyl chain lengths. The octameric micelles form a unique coiled-coil structure, with the acyl chains in a nearly frozen conformation inside the cylindrical assemblies. Two extreme models with helices either all parallel or in an alternating orientation suggest that the alternating orientation is energetically more favorable. The models suggest several new directions for further diversifying this new class of detergents for the structural studies of membrane proteins.