Title: Designing Biomolecular Crystals by Engineering Protein and DNA Building Blocks
Time: 11:00 a.m.
Location: Room 202 MRB
Presenter: Professor Christopher Snow (Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado)
Controlled self-assembly of proteins via design of protein-protein interfaces is an active research frontier. The Snow lab is developing molecular design strategies for engineering functional biomolecular crystals. One key virtue of having a crystalline design target is the ready availability of detailed structural information via X-ray diffraction. Put simply, we can rapidly check if our designed proteins adopt the intended structures. Ultimately, we use both structure-guided computational protein design methods and all-atom molecular simulation to guide the selection of new biomolecular crystal building blocks. A key motivation for nano-biotechnology efforts is the creation of designer materials in which the assembly acts to organize functional domains in three dimensions. The resulting crystalline materials can have myriad applications. For example, organizing enzymes within a 3D scaffold can lead to optimized catalysis. Organizing gold nanoparticles within a 3D scaffold can lead to anisotropic plasmonic properties and templated growth of inorganic nanostructures. Conditional retention of fluorescent proteins can lead to novel biosensor modalities. Additionally, the structure of guest molecules may be interrogated via X-ray diffraction if the guest is arrayed precisely by a host crystal. Ultimately, engineered crystals containing protein building blocks may serve as a robust alternative to DNA assemblies for the programmed placement of macromolecules within atomically precise materials.