The physical basis for protein folding is considered by many to be one of the greatest unknowns in science. Protein folding is coupled with several cellular functions, including protein trafficking and the regulation of cell growth and differentiation. The inability of a protein to fold properly and remain folded can contribute to several diseases, including cystic fibrosis, some forms of cancer, and sickle cell anemia. Understanding protein folding will provide invaluable information that could lead to treatments or the prevention of diseases associated with protein aggregation and misfolding.
Protein folding is a heterogeneous process; ensemble studies have indicated structural heterogeneity throughout the folding process. However, ensemble folding studies are often unable to reveal folding intermediates with small subpopulations or short lifetimes. Single molecule studies can probe the ensemble to reveal such intermediates and can provide the opportunity to follow a single protein on its folding pathway. This project uses cytochrome c, a small, soluble heme containing electron transfer protein, in order to study protein folding on the single molecule level.
