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Coarse-grained molecular dynamics simulations of the E. coli outer membrane proteins FhuA, LamB, NanC, OmpA and OmpF in a POPE/POPG (3:1) bilayer were performed to characterise the diffusive nature of each component of the membrane. At small observation times (<10 ns) particle vibrations dominate phospholipid diffusion elevating the calculated values from the longer time-scale bulk value (>50 ns) of 8.5×10(-7) cm(2) s(-1). The phospholipid diffusion around each protein was found to vary based on distance from protein. An asymmetry in the diffusion of annular lipids in the inner and outer leaflets was observed and correlated with an asymmetry in charged residues in the vicinity of the inner and outer leaflet head-groups. Protein rotational and translational diffusion were also found to vary with observation time and were inversely correlated with the radius of gyration of the protein in the plane of the bilayer. As the concentration of protein within the bilayer was increased, the overall mobility of the membrane decreased reflected in reduced lipid diffusion coefficients for both lipid and protein components. The increase in protein concentration also resulted in a decrease in the anomalous diffusion exponent α of the lipid. Formation of extended clusters and networks of proteins led to compartmentalisation of lipids in extreme cases.

Original publication

DOI

10.1371/journal.pcbi.1003033

Type

Journal article

Journal

PLoS Comput Biol

Publication Date

04/2013

Volume

9

Keywords

Algorithms, Bacterial Outer Membrane Proteins, Cell Membrane, Computational Biology, Diffusion, Escherichia coli, Lipid Bilayers, Lipids, Membrane Lipids, Molecular Dynamics Simulation, Phospholipids, Protein Conformation, Protein Interaction Mapping, Proteins, Software