New Science paper: Designed 2-D protein arrays

A new Science paper is out from IPD faculty Dr. David Baker titled Design of ordered two-dimensional arrays mediated by noncovalent protein-protein interfaces. Read the abstract below and the article at the link: http://www.sciencemag.org/content/348/6241/1365

We describe a general approach to designing two-dimensional (2D) protein arrays mediated by noncovalent protein-protein interfaces. Protein homo-oligomers are placed into one of the seventeen 2D layer groups, the degrees of freedom of the lattice are sampled to identify configurations with shape-complementary interacting surfaces, and the interaction energy is minimized using sequence design calculations. We used the method to design proteins that self-assemble into layer groups P 3 2 1, P 4 2(1) 2, and P 6. Projection maps of micrometer-scale arrays, assembled both in vitro and in vivo, are consistent with the design models and display the target layer group symmetry. Such programmable 2D protein lattices should enable new approaches to structure determination, sensing, and nanomaterial engineering.

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Shown is a 2D array with P 6 symmetry. (Left) the P 6 lattice has two degrees of freedom available for sampling. Sixfolds are represented by hexagons. (Middle) Computationally designed 2D array. (Right) Electron microscopy of designed P 6 array.