Abstract
A full understanding of the function of many proteins can only be obtained if different conformations and transitions between them can be monitored in aqueous solution, with adequate temporal resolution. Despite the importance of conformational dynamics, monitoring domain motions of single proteins remains challenging experimentally. Established techniques to determine these conformational changes typically require site-directed chemical modification. The work presented here introduces an approach that traps single unmodified proteins in solution in a plasmonic hotspot and makes it possible to follow changes in protein conformation by concomitant changes in refractive index that can be detected and monitored for minutes to hours with a temporal resolution in the microsecond range.
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