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Abstract
Publisher Summary The elucidation of protein–lipid interactions is of great importance for understanding the organization and function of biomembranes including sarcoplasmic reticulum (SR) . The membrane lipid can influence the physical state and function of intrinsic membrane proteins. On the other hand, the presence of intrinsic proteins can modify the properties of membrane lipids. One of the best systems for studying the protein–lipid interactions is provided by the membrane reconstituted from purified SR Ca-ATPase and a chemically well-defined phospholipid. The method of Ca-ATPase reconstitution using exogenous phospholipids has been well established and biochemical and enzymatic investigations have been extensively carried out. This chapter presents a study on protein–lipid interaction in sarcoplasmic reticulum and phospholipid-replaced membranes. The study investigates the temperature-dependence of rotational mobility of the Ca-ATPase protein molecule and alkyl chain flexibility of bulk and boundary lipids using ESR-spin labelling techniques. It also investigates the structural fluctuation of the Ca-ATPase molecule measured by hydrogen–deuterium exchange kinetics.
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