Lipid-protein interaction in the phosphatidylcholine exchange protein.

Abstract
Incorporation of 2-acyl spin-labeled lecithin into the phosphatidylcholine exchange protein from bovine liver results in an immobilization of the spin-label at the methyl and the carboxyl terminal end of the acyl chain. The nitroxide group on the protein-bound lecithin molecule is not accessible to ascorbate. This suggests that lecithin is buried in a pocket on the protein, which effectively shields the acyl chains from the medium.

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