Abstract
The transition path (TP) is the tiny fraction of an equilibrium molecular trajectory that connects two states of a system, and contains all mechanistic details of the barrier-crossing process. It is a uniquely single-molecule property, and has not yet been observed for any system. In the case of protein folding, the theoretically-predicted duration of the TP is so short (∼1 microsecond) that measurement of just the average TP time is challenging for single molecule experiments. We previously estimated an upper bound for the TP time of ∼200 microsecond for folding of the two-state, protein G using single molecule Förster-resonance-energy-transfer (FRET) spectroscopy.
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