The first goal of our research program is to understand the pathways of protein folding. With cytochrome c as a model system, we discovered that the folding of a small single domain protein involves two phases. In the second phase, it is followed by fine-tuning of the polypeptide architecture through a thermodynamically controlled process. This biphasic mechanism guarantees the efficiency and fidelity of the folding process. The current focus is to dissect the folding pathway of myoglobin to test the generality of this model.
Nitric oxide is one of the most important molecules in life.
It acts as a signaling molecule as well as a cytotoxic agent in vivo. Nitric oxide interacts with a wide variety of heme containing proteins by binding to its heme prosthetic group, cysteines or tyrosines. Hierarchical Folding of Cytochrome c Syun-Ru Yeh and Denis L. Rousseau, Nature Struct. Chem., 1679-1684, 2000. Biol . 5, 222-228, 1998.