Abstract
To understand the molecular mechanism of protein folding, it is necessary to reveal the dynamics of single proteins from the unfolded state to the folding transition state. We therefore developed a new system that can detect fluorescence signals from free single proteins for extended time periods. The system enabled us to characterize a slow conformational dynamics for the unfolded state of cytochrome c. Furthermore, we proposed a method to estimate the equilibration time for the intermediate state of protein folding.
