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.
In order to characterize protein intermediates on the folding pathway, single molecule (SM) spectroscopy is necessary. Ensemble folding studies provide average signals while SM folding studies allow for the observation of a single protein on its folding pathway, revealing subpopulations and transiently populated intermediates. This project uses cytochrome c, a small, soluble heme containing electron transfer protein in order to study protein folding on the single molecule level.
Image of single dye labeled proteins and corresponding time trace
Horse heart cytochrome c
