We believe in a protein folding code that dictates how a protein folds into its biologically active conformation. To test our understanding of this protein folding code, we design an amino acid sequence that will fold into a desired conformation. We then produce the protein chemically or biologically, and characterize its structure and thermodynamic properties using NMR spectroscopy, circular dichroism spectroscopy, fluorescence spectroscopy, calorimetry, and analytical ultracentrifugation. This iterative process of design and production of a protein followed by rigorous biophysical characterization is called de novo protein design and allows us to refine the protein folding code. Intracellular Communication Networks Life requires proper communication.
Communication networks exist within a cell that allows for proper cell life.
This intracellular communication involves a complex network of interactions between proteins and other biomolecules. Many of these networks are composed of protein-protein interactions that need to be tightly regulated for proper cell life. To understand how these networks are regulated, we will isolate proteins known to regulate intracellular communication networks and determine their structural, thermodynamic, and kinetic properties. The results of this work will identify essential features involved in the misregulation of these networks and identify possible therapeutic routes. Res. , in press.