Protein–Lipid Docking

Protein–lipid interactions are stabilized by the formation of intermolecular hydrogen bonds, van der Waals interactions, hydrophobic interactions, and ionic bridges (especially aspartate or glutamate residues) between the protein and lipid ligand. Profacgen makes use of the state-of-the-art computational software tools to predict these protein–lipid interactions. The lipid binding sites of a protein can be deduced from its amino acid sequence, and/or predicted from its three-dimensional structure using molecular docking protocols. Our docking method combines sequence and structure information, and explores the most energetically favorable protein-lipid complex. The scoring function is specifically designed to allow for the prediction of lipid distortion and protein conformational changes associated with the binding event. Experiment-derived restraints can also be applied to limit the search space. The structures with best values of binding energies are clustered and representatives of the largest clusters are selected for structural optimization by energy minimization before being presented to the customer. The stability of docked complexes can be further tested through molecular dynamic simulations.

		From	To	From	To	From	To
Monday	Open
Tuesday	Open
Wednesday	Open
Thursday	Open
Friday	Open
Saturday	Open
Sunday	Open