Our goal is to perform realistic molecular modeling studies relating to protein stability, function, and folding. Protein folding is one of the fundamental unsolved problems in molecular biology. A protein must assume a stable and precisely ordered conformation to perform its biological function properly. Although much is known of the structural details of the native folded conformation of proteins, very little is known about the actual folding process. An understanding of protein folding has important implications for all biological processes, including protein degradation, protein translocation, aging, and human diseases, including cancer and amyloid diseases. The solution to the protein folding problem also has applications in the human genome project and biotechnology. Given that protein folding is of such widespread importance to human health and the fact that experimental approaches only provide limited amounts of information on the structural transitions and interactions occurring during protein folding, we are using computer simulation methods in an attempt to delineate the important forces acting during this process. We have also become involved in biomaterial and biosensor design, making use of what we have learned in our structural, dynamics, and folding studies of well-studied globular proteins. Other areas of interest include: structural and dynamical consequences of amino acid mutations, hydrophobic hydration, force field and software development, and dynameomics.