TCB Publications - Abstract
Feng Zhou and Klaus Schulten. Molecular dynamics study of the activation of phospholipase A2 on a membrane surface. PROTEINS: Structure, Function, and Genetics, 25:12-27, 1996.
with a lipid membrane is investigated as a mechanism which enhances the overall activity of the enzyme. For this purpose the interaction of the enzyme phospholipase with a DLPE membrane monolayer surface has been studied by means of molecular dynamics simulations. Two enzyme-membrane complexes, a loose and a tight complex, are considered. For comparison, simulations are also carried out for the enzyme in aqueous solution. The conformation, dynamics and energetics of the three mentioned systems are compared and the interactions between the protein and lipid molecules are analyzed. Free energies of solvation are calculated for the lipid molecules in the enzyme-membrane interface. Along with the calculated dielectric susceptibility at this interface, the results indicated the desolvation of lipids in a tightly bound, but not in a loosely bound protein-membrane complex. The desolvated lipids are found to interact mainly with hydrophobic protein residues, including Leu-2, Val-3, Ala-18, Leu-19, Phe-24, Val-31 and Phe-70. The results explain also why the turnover rate of phospholipase complexed to a membrane is enhanced after a critical amount of negatively charged reaction product is accumulated. Download Full Text
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