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Huddy, Hsia, Kibler, Xu & 27 others in the Nobel Prize winning group of David Baker have designed standardized protein building blocks that self assemble into a wide range of nanostructures. The building blocks attach to each other at engineered sites and angles, and come in various sizes.

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IB Tomasic, MC Metcalf, AI Guce, NE Clark, SC Garman. J. Biol. Chem. 2010 doi: 10.1074/jbc.M110.118588
The human lysosomal enzymes α-galactosidase and α-N-acetylgalactosaminidase share 46% amino acid sequence identity and have similar folds. Using a rational protein engineering approach, we interconverted the enzymatic specificity of α-GAL and α-NAGAL. The engineered α-GAL retains the antigenicity but has acquired the enzymatic specificity of α-NAGAL. Conversely, the engineered α-NAGAL retains the antigenicity but has acquired the enzymatic specificity of the α-GAL enzyme. Comparison of the crystal structures of the designed enzyme to the wild-type enzymes shows that active sites superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

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The Capsid of a virus is its outer shell or "skin". Viruses have evolved intricate and elegant ways to assemble capsid protein chains into complete, usually spherical capsids, often with icosahedral symmetry. Pictured is an extremely simplified model of a capsid, where a single enlarged atom represents each of the 360 protein chains in the capsid of the Simian Virus 40 (SV40), a member of a group of cancer-causing viruses that has been extensively researched for decades.

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