Orientational Fluctuations of Melittin in Lipid Membranes as Detected by Time-Resolved Fluorescence Anisotropy Measurements

Abstract

Time-resolved fluorescence anisotropy of the single tryptophan residue of melittin was measured to assess the orientational fluctuations of the protein in lipid mebranes above and below the lipid phase transition temperature. The method described may be applicable for the general characterization of protein fluctuations in lipid membranes.