Fluorescence studies showed that glucagon binds to a variety of micellar lipids. By means of ultracentrifugation and quasi-elastic light-scattering, it was found that stoichiometrically well defined complexes were formed between glucagon and perdeuterated dodecylphosphocholine micelles consisting of one glucagon molecule and approx. 40 detergent molecules. Well resolved 1H-NMR spectra were obtained for glucagon in the deuterated micelles. Studies of nuclear Overhauser effects between individually assigned protons in different regions of the amino acid sequence indicated that micelle-bound glucagon adopts a well defined, predominantly extended conformation. Evidence obtained from circular dichroism indicates that the conformation of glucagon bound to various micellar lipids is largely independent of the type of lipid and, furthermore, appears to be very similar to that of glucagon bound to lipid bilayers.