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- W4238075764 abstract "In recent experiments [T. Basta et al., Proc. Natl. Acad. Sci. U.S.A. 111, 670 (2014)] lipids and membrane proteins were observed to self-assemble into membrane protein polyhedral nanoparticles (MPPNs) with a well-defined polyhedral protein arrangement and characteristic size. We develop a model of MPPN self-assembly in which the preferred symmetry and size of MPPNs emerge from the interplay of protein-induced lipid bilayer deformations, topological defects in protein packing, and thermal effects. With all model parameters determined directly from experiments, our model correctly predicts the observed symmetry and size of MPPNs. Our model suggests how key lipid and protein properties can be modified to produce a range of MPPN symmetries and sizes in experiments." @default.
- W4238075764 created "2022-05-12" @default.
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- W4238075764 date "2016-09-21" @default.
- W4238075764 modified "2023-10-12" @default.
- W4238075764 title "Symmetry and Size of Membrane Protein Polyhedral Nanoparticles" @default.
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- W4238075764 doi "https://doi.org/10.1103/physrevlett.117.138103" @default.
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