|The primary interest of our group is the study of protein folding as a means to uderstanding the relationships among sequence, structure, stability and folding kinetics and as a way to further our ability to accomplish de novo protein design. Our approach has been to design, de novo, a helical hairpin peptide, alpha-t-alpha, to use as a model system for folding intermediates at the level of secondary structure association and as a test bed for de novo protein design. Most of the reseach in our group focuses on studying the physical properties of our model system, on redesigning alpha-t-alpha to investigate specific questions related to protien design or on cloning and expression of the molecule.
- Design, structure and stability of alpha-t-alpha.
- Stabilization of helices by association.
- Hydrogen exchange as a tool to examine stability and conformation in peptides and proteins, particularly in strange environments.