Infrared Spectroscopic Characterization of cPLA2Á C2 Domain Public
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Group IV cytosolic phospholipase A2Á (cPLAZÁ) hydrolyzes membrane phospholipids to produce arachidonic acid and lysolipid. The C2 domain of the enzyme is involved in the Ca2+ dependent translocation of the enzyme to the membrane and has a structure of 8 anti-parallel Â sheets composed of 132 amino acids. Ceramide-1-phosphate (C1P) enhances the association of the C2 domain with membranes. This research project aims to understand the binding properties and secondary structural changes of the cPLA2Á C2 domain in the presence of phosphatidylcholine (PC). We optimized the protein expression conditions to obtain the cPLA2Á C2 domain un-aggregated and in sufficient quantity. Initial FTIR-ATR experiments confirmed the Â-sheet structure of the protein alone and in the presence of PC.
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