Recent advances in materials synthesis have yielded nanoscale building blocks for the construction of devices with unprecedented capabilities. The ability to tailor the size and associated physical properties of these components has already led to advances in solar cell technology, single molecule electronics, drug delivery systems, molecular machines, and many other areas. However, with these exciting materials comes an urgent need for patterning techniques that can position them into functional assemblies. These methods must possess exquisite resolution (<5 nm feature size) and the ability to maintain distance relationships between the components after they are positioned. In addition, it is necessary to establish long range order to interface these components with existing device structures.
      A relative new set of tools for this purpose has been provided by self-assembling biomolecules. These structures could solve a number of the patterning difficulties in nanoscience, as many biomolecules form rigid supramolecular structures with nanoscale feature sizes. With this approach emerges a new set of challenges, however, as the size distribution of the assemblies is often uncontrolled, and the attachment of biomolecular structures to electrical contacts is difficult. It should also be noted that the incorporation of inorganic particles, conducting polymers, and other components of material interest into biological matrices is by no means a trivial task. To address these challenges, a central theme in our lab is the development of efficient strategies to append new electronic and optical functionality to structural proteins. Once obtained, these bioconjugates are assembled into hybrid structures with targeted properties.  Although many biological structures will undoubtedly find use in materials construction as these challenges are solved, the protein shells of viruses provide an exceptionally promising set of building blocks. In addition to possessing nanoscale dimensions overall, the protein subunits that comprise the capsid shells provide periodically spaced attachment points along a rigid and stable scaffold.
      In parallel, significant efforts are directed toward an expansion of the synthetic toolkit that is available for bioconjugation. Through a combination of protein expression, purification, and characterization with organic synthesis and physical organic chemistry, several powerful new strategies have been developed. Each of these new reactions has expanded both the range of bioconjugates that can be prepared, as well as the applications for which they can be used.