Abstract
Currently there is much interest in the interactions between lipids and membrane proteins or peptides containing up to about 30 amino acids. New physical methods for such studies are presently being developed or improved, such as surface plasmon resonance techniques fit for lipid bilayers, titration calorimetry and solid-state NMR methods, in particular magic angle sample spinning. A breakthrough in the crystallization of membrane proteins was recently established, in which a lipid cubic phase was utilized, thus allowing the determination of the integral protein structure to a resolution of 2.0 A. The physicochemical properties of the lipid bilayer play an important role in many biomembrane processes, such as membrane protein folding and peptide-induced membrane fusion.
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