Before revision:  We used this technique to explore the dynamics of the  heat shock protein 90 (Hsp90) and find (beside the well-known fast dynamics in the range netween 0.1 and 10 s) states with very long dwell times (linked to rarely visited states) in the minute timescale, which could indicate, for instance, pathways to protein denaturation. Our plasmon ruler based method will enable to access the full complexity of correlated local and global conformational dynamics on the level of individual proteins and therefore extend and complement the current "structure / function" paradigm with a novel "structure / timescale / function" description.
After revision:  We used this technique to explore the dynamics of the heat shock protein 90 , which is known to show open and closed conformations. Our measurements confirm the previously known conformational dynamics with transition times in the second to minute time scale and reveals new dynamics on the level of individual proteins and therefore extend and complement the current "structure / function" paradigm with a novel "structure / timescale / function" description.