The long-term goal of Dr. Robert Fox's laboratory is to understand the structure and function of protein molecules in terms of their chemistry and physics. Their approach is to study the folding and function of natural proteins, and to learn from the design of new protein molecules. The laboratory has joined the new field of synthetic biology, and is engineering new proteins and signaling pathways to develop novel therapeutic approaches.

A cure for HIV-1 infection requires the elimination of all cells that have the virus integrated into their genome. The Fox laboratory is developing a protein-based molecular computer that will induce apoptosis when it detects the presence of the HIV-1 virus in a cell. This novel strategy will be extended to other viruses.

The laboratory is developing miniproteins, small disulfide-rich folded proteins that bind tightly to flavivirus E proteins and block cell entry.

The Fox lab is investigating the structural basis of HIV-1 Rev recognition of its RRE RNA target and host cell factors using NMR spectroscopy and X-ray crystallography.

The stress response in E. coli and other bacteria involves chaperones, transcription regulators, and enzymes. The lab is taking a structural genomics approach to understand the role of stress proteins that do not yet have a documented function.

Staphylococcal nuclease has long been a focus of their studies of protein folding and stability using NMR spectroscopy and other physical methods. The laboratory has developed a chemical cleavage technique to investigate the structure of equilibrium folding intermediates. They also investigate the role of amino acid sequence in favoring particular structural elements in globular proteins.