Dr. Landry has worked for fifteen years on the structure and function of heat shock proteins, which are produced by all cells and organisms under stress. Since antigen-processing cells constantly present both foreign and self proteins to T cells, heat shock proteins are abundantly presented in areas of infection, inflammation, and trauma. Immunosuppressive responses triggered by heat shock proteins have already been shown to prevent arthritis and diabetes. A similar mechanism in humans could dictate one's chances of developing arthritis and diabetes, as well as other autoimmune diseases, such as multiple sclerosis, myasthenia gravis, inflammatory bowel disease, lupus, Sjogren's syndrome, scleroderma, sarcoidosis, and possibly even atherosclerosis and heart disease. An important aspect of our approach to understanding biological processes is to analyze the structure and dynamics of proteins.
Proteins are chains of amino acids.
Recently, we've begun to describe the structural fluctuations in the disordered regions with the goal of understanding how these fluctuations affect the binding of heat shock proteins to each other. Eventually, these studies will show how heat shock proteins promote the proper folding and assembly of other proteins. Some evidence suggests that heat shock proteins are involved in the development and propagation of amyloid diseases such as Alzheimer's disease and Mad Cow disease, in which certain proteins misfold into a toxic form. Animation of various conformations of the GroES mobile loop.