High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.

Previously, the size and stoichiometry of mixed micelles of perdeuterated dodecylphosphocholine and melittin were characterized and the 1H NMR spin systems of most amino acid residues of micelle-bound melittin identified. One- and two-dimensional 1H-1H Overhauser experiments have now been used to obtain qualitative information on intramolecular proton-proton distances. These data show that the N-terminal and the C-terminal segments of melittin form two spatially distinct, compact domains; using lipid spin labels these could be located near the micelle surface. For the C-terminal domain a detailed conformation was determined by using the distance contraints from the Overhauser studies as input for a distance geometry algorithm.