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Faculty Profile

Robert FoxRobert Fox

Professor
Department of Biology and Biochemistry

Office: Science & Engineering Research Center, 4011
Contact: rofox@uh.edu - (713) 743-9300

Education: Ph.D., Yale University

The Physical Basis of Protein Structure and Function

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.

Synthetic Biology

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.

Development of Antiviral Miniproteins Targeting Cell Entry

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

Structural Biology of the HIV-1 Rev Protein

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.

Structural Genomics of E. coli Stress Proteins

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.

Protein Folding & Protein Engineering

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.

  • Characterizing the Role of Ensemble Modulation in Mutation-Induced Changes in Binding Affinity. Manson, A., Whitten, S. T., Ferreon, J. C., Fox, R. O. and Hilser, V. J. J. Am. Chem. Soc. 131, 6785-93 (2009).
  • Overexpression and functional characterization of the extracellular domain of the human alpha1 glycine receptor. Z. Liu, G. Ramanoudjame,R.O. Fox, V. Jayaraman, M. Kurnikova, M. Cascio Biochemistry 47, 9803%u20139810; (2008).
  • Exploring the impact of conformational bias on the binding of peptides to the SEM-5 SH3 domain. S.T. Whitten, H.-W. Yang, R.O. Fox, and V.J. Hilser. Protein Science 17, 1200-1211; (2008).
  • The crystal structure of the E. coli stress protein YciF. A. Hindupur, D. Liu, Y. Zhao, H.D. Bellamy, M.A. White, and R.O. Fox. Protein Science 15, 2605-11; (2006).
  • NMR solution structure and backbone dynamics of domain III of the E-protein of tick-borne Langat flavivirus, suggests a specific epitope. M. Mukherjee, K. Dutta, M. A. White, D. Cowburn and R. O. Fox.Protein Science 15, 1342-55; (2006).