Abstract
Recent biophysical studies using a range of physical and spectroscopic techniques of both biomembranes and various lipid–water (vesicle) systems are described. The nature of lipid–protein interactions in some natural and model biomembranes has been examined with regard to the extent of lipid perturbation and protein conformational changes. The application of second-derivative and fourth-derivative infrared spectroscopy to these systems indicates clearly the bands associated with the secondary structure and also the weak bands associated with the minor amide components of the membrane proteins. The technique also provides evidence for the effects of intrinsic proteins on the lipid carbonyl groups when the lipid is below its Tc transition temperature.Studies of phospholipid polymers in vesicle form and in Langmuir–Blodgett films are discussed. The introduction of new biomembrane-mimetic surfaces are also described. The latter are used to study protein and cell adsorption to particular phospholipid polar groups.
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