| Abstract | Multiscale molecular dynamics simulations of the UraA symporter in phospholipid bilayers consisting of: 1) 1-palmitoyl 2—oIeoyl-phosphatidylcholine (POPC); 2) 1-palmitoyl 2—oleoyI-phosphatidylethanolamine (POPE); and 3) a mixture of 75% POPE, 20% 1-palmi-toyl 2—oleoyl-phosphatidylglycerol (POPG); and 5% 1-palmitoyl 2—oleoyI-diphosphatidylgly-cerol/cardiolipin (CL) to mimic the lipid composition of the bacterial inner membrane, were performed using the MARTINI coarse-grained force field to self-assemble lipids around the crystal structure of this membrane transport protein, followed by atomistic simulations. |
| Atomistic molecular dynamics simulations | Atomistic molecular dynamics simulations |
| Coarse-grained molecular dynamics simulations | Coarse-grained molecular dynamics simulations |
| Membrane proteins in lipid bilayers | Molecular dynamics simulations provide a powerful tool to analyze the structure and dynamics of membrane proteins in lipid bilayers of defined composition [4]. |
| Membrane proteins in lipid bilayers | A molecular dynamics simulation of LacY, in various lipids identified specific interactions between the lipid head-groups and sites on the protein [70]. |
| Author Summary | The inferences provided by the extensive molecular dynamics simulations reported herein constitute a first step in this direction. |
| Molecular Dynamics Simulations | Molecular Dynamics Simulations |
| Supporting Information | Summary of all the molecular dynamics simulations of coarse-grained representations of opioid receptors reported in this manuscript. |