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Single-molecule F\"orster Resonance Energy Transfer (smFRET) is ideallysuited to resolve the dynamics of biomolecules. A significant challenge to dateis capturing and quantifying the exchange between multiple conformationalstates, mainly when these dynamics occur on the sub-millisecond timescale. Manymethods for the quantitative analysis are challenged if more than two statesare involved, and the appropriate choice of the number of states in the kineticnetwork is difficult. An additional complication arises if dynamically activemolecules coexist with solely static molecules in similar conformationalstates. To address these problems, we developed an integrative analysisframework that combines the information from FRET-lines, time-correlated singlephoton counting, and fluorescence correlation spectroscopy. While individually,these methodologies provide ambiguous results for quantitatively characterizethe dynamics in complex kinetic networks, the global analysis enables accuratedetermination of the number of states, their kinetic connectivity, and thetransition rate constants. To challenge the potential of smFRET to studymulti-state kinetic networks, we benchmark the framework using synthetic dataof three-state systems with different kinetic connectivity and interconversionrates.

Unraveling multi-state molecular dynamics in single-molecule FRET experiments -- Part II: Quantitative analysis of multi-state kinetic networks