Abstract
The hydrophobic character of the trimethyl group of sodium 2,2-dimethyl-2-silapentane-5-sulfonate, makes it an effective PMR probe for apolar sites on proteins and membranes. By comparing the spin-spin relaxation rates of the free and bound probe the extent and strength of the interaction can be qualitatively compared for bovine serum albumin, membranes from Micrococcus lysodeikticus and for different fractions isolated from this membrane. It is concluded that this membrane has hydrophobic sites on or near its surface and that the number of such sites is sensitive to the ionic composition and to the pH of its aqueous environment. Removal of lipid from the membrane greatly increased the binding of the probe, while vesicular preparations of the lipid fraction itself gave no evidence of an interaction with the probe. The results are discussed in terms of protein-lipid-water interactions.
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