Over the past decade spectroscopic methods (fluorescence, ESR, and NMR) have been used to provide new information about the molecular dynamics of lipid-lipid and lipid-protein interactions in membranes. The various methods of characterizing isotropic and anisotropic motion are described. Lipid bilayers are highly dynamic, with rapid acyl chain motion and rapid lateral diffusion in the plane of the membrane. In membranes where proteins penetrate through the bilayer, a large hydrophobic surface area exists in contact with the bilayer lipids. Lipids at the protein interface are in dynamic equilibrium with the remaining pools of bilayer. The protein has been shown spectroscopically to have some influence on the dynamics of the nearest neighbor lipids, leaving the rest of the bilayer relatively unperturbed. Evidence is summarized that, in some cases, the lipid composition in the interfacial region is influenced by the protein.
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