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We use plasmon rulers to follow the conformational dynamics of a singleprotein for up to 24 h at a video rate. The plasmon ruler consists of two goldnanospheres connected by a single protein linker. In our experiment, we followthe dynamics of the molecular chaperone heat shock protein 90, which is knownto show open and closed conformations. Our measurements confirm the previouslyknown conformational dynamics with transition times in the second to minutetime scale and reveals new dynamics on the time scale of minutes to hours.Plasmon rulers thus extend the observation bandwidth 3/4 orders of magnitudewith respect to single-molecule fluorescence resonance energy transfer andenable the study of molecular dynamics with unprecedented precision.

Conformational dynamics of a single protein monitored for 24 hours at video rate