Abstract
The ability to resolve accurate distance fluctuations on the single-molecule level concurrently with the timescale of the dynamics is vital to the understanding of many biological and biochemical reactions. Förster resonance energy transfer (FRET) in combination with single-molecule fluorescence microscopy has grown into one of the most popular tools to study the kinetics of such processes in real-time. Dynamics is the link that connects the function of a protein with its structure and function. The molecular mechanisms involved strongly depend on the conformation as well as inter- and intramolecular dynamics.
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