Abstract
The nature of the Ca-phosphatidylserine complex has been investigated by nuclear magnetic resonance and X-ray diffraction. Ca + binding to the lipid polar group involves the phosphate group and liberates water of hydration from the interbilayer space and from the binding sites of the lipid polar group. Consequently the packing of the lipid polar group becomes tighter and the segmental motion of the phosphate group is reduced. A tightly self-associated, dehydrated (“hydrophobic”) Ca-phosphatidylserine complex is formed with crystalline hydrocarbon chains. The overall bilayer structure is retained. The interaction of phosphatidylserine bilayers with Ca 2+ is equivalent to an isothermal transition of the bilayer from the liquid crystalline to the crystal state.
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