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  • Title: Spin label saturation transfer EPR determinations of the stoichiometry and selectivity of lipid-protein interactions in the gel phase.
    Author: Horváth LI, Brophy PJ, Marsh D.
    Journal: Biochim Biophys Acta; 1993 Apr 22; 1147(2):277-80. PubMed ID: 8386549.
    Abstract:
    Lipid-protein interactions with the myelin proteolipid protein incorporated in the gel phase of dimyristoylphosphatidylcholine bilayers have been studied by saturation transfer EPR spectroscopy of spin-labelled phospholipids. The integrated intensities of the saturation transfer EPR spectra from spin-labelled phosphatidylcholine are linearly dependent on the protein/lipid ratio, and correspond to a fixed stoichiometry of approximately 11 lipids per monomer associated with the protein in the gel phase. The normalized saturation transfer intensities of spin-labelled phosphatidic acid, on the other hand, display a non-linear dependence on the protein/lipid ratio that can be described well by a selectivity for interaction with the protein in the gel phase with an average association constant relative to phosphatidylcholine of approx. 5.2. These values for the stoichiometry and selectivity of lipid-protein interaction in the lipid gel phase obtained from saturation transfer EPR spectroscopy are comparable to those found previously in fluid phase lipids by conventional EPR spectroscopy.
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