Computational design of self-assembling protein nanomaterials with atomic level accuracy.
We describe a general computational method for designing proteins that self-assemble to a desired symmetric architecture. Protein building blocks are docked together symmetrically to identify complementary packing arrangements, and low-energy protein-protein interfaces are then designed between the building blocks in order to drive self-assembly. We used trimeric protein building blocks to design a 24-subunit, 13-nm diameter complex with octahedral symmetry and a 12-subunit, 11-nm diameter complex with tetrahedral symmetry. The designed proteins assembled to the desired oligomeric states in solution, and the crystal structures of the complexes revealed that the resulting materials closely match the design models. The method can be used to design a wide variety of self-assembling protein nanomaterials.
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Neil P
NP
King
William
W
Sheffler
Michael R
MR
Sawaya
Breanna S
BS
Vollmar
John P
JP
Sumida
Ingemar
I
André
Tamir
T
Gonen
Todd O
TO
Yeates
David
D
Baker
D002850:Chromatography, Gel; D003001:Cloning, Molecular; D019295:Computational Biology; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006860:Hydrogen Bonding; D008854:Microscopy, Electron; D008958:Models, Molecular; D008970:Molecular Weight; D009154:Mutation; D049329:Nanostructures; D015202:Protein Engineering; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
D021122:Protein Subunits; D011506:Proteins