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      Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments.

      Proceedings of the National Academy of Sciences of the United States of America
      Amino Acid Sequence, Biopolymers, Crystallization, Proteins, chemistry

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          Abstract

          A general strategy is described for designing proteins that self assemble into large symmetrical nanomaterials, including molecular cages, filaments, layers, and porous materials. In this strategy, one molecule of protein A, which naturally forms a self-assembling oligomer, A(n), is fused rigidly to one molecule of protein B, which forms another self-assembling oligomer, B(m). The result is a fusion protein, A-B, which self assembles with other identical copies of itself into a designed nanohedral particle or material, (A-B)(p). The strategy is demonstrated through the design, production, and characterization of two fusion proteins: a 49-kDa protein designed to assemble into a cage approximately 15 nm across, and a 44-kDa protein designed to assemble into long filaments approximately 4 nm wide. The strategy opens a way to create a wide variety of potentially useful protein-based materials, some of which share similar features with natural biological assemblies.

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          Author and article information

          Journal
          11226219
          30118
          10.1073/pnas.041614998

          Chemistry
          Amino Acid Sequence,Biopolymers,Crystallization,Proteins,chemistry
          Chemistry
          Amino Acid Sequence, Biopolymers, Crystallization, Proteins, chemistry

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