@article {46845,
	title = {Design of ordered two-dimensional arrays mediated by noncovalent protein-protein interfaces.},
	journal = {Science},
	volume = {348},
	year = {2015},
	month = {2015 Jun 19},
	pages = {1365-8},
	abstract = {<p>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 21 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.</p>
},
	doi = {10.1126/science.aaa9897 },
	author = {Gonen, Shane and DiMaio, Frank and Gonen, Tamir and Baker, David}
}
@article {45637,
	title = {High thermodynamic stability of parametrically designed helical bundles.},
	journal = {Science},
	volume = {346},
	year = {2014},
	month = {2014 Oct 24},
	pages = {481-5},
	abstract = {<p>We describe a procedure for designing proteins with backbones produced by varying the parameters in the Crick coiled coil-generating equations. Combinatorial design calculations identify low-energy sequences for alternative helix supercoil arrangements, and the helices in the lowest-energy arrangements are connected by loop building. We design an antiparallel monomeric untwisted three-helix bundle with 80-residue helices, an antiparallel monomeric right-handed four-helix bundle, and a pentameric parallel left-handed five-helix bundle. The designed proteins are extremely stable (extrapolated ΔGfold \&gt; 60 kilocalories per mole), and their crystal structures are close to those of the design models with nearly identical core packing between the helices. The approach enables the custom design of hyperstable proteins with fine-tuned geometries for a wide range of applications.</p>
},
	issn = {1095-9203},
	doi = {10.1126/science.1257481},
	author = {Huang, Po-Ssu and Oberdorfer, Gustav and Xu, Chunfu and Pei, Xue Y and Nannenga, Brent L and Rogers, Joseph M and DiMaio, Frank and Gonen, Tamir and Luisi, Ben and Baker, David}
}
