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. Author manuscript; available in PMC: 2019 Feb 16.
Published in final edited form as: J Mol Biol. 2017 May 23;430(4):424–437. doi: 10.1016/j.jmb.2017.05.021

Figure 2. Single-molecule FRET measurements of membrane protein folding.

Figure 2

(A) Example trajectory of a membrane protein undergoing folding and unfolding transitions through the confocal excitation volume. (B) Mistic in a micelle environment unfolded with urea (triangles). (C) Histogram of FRET efficiencies from recorded single-molecule bursts. Low FRET efficiencies represent the fraction of unfolded molecules (green), while high FRET efficiencies represent folded molecules (red). The mid-range FRET efficiencies arise from molecules undergoing fast folding and unfolding transitions during single bursts, reflecting the unfolding and folding rates, ku and kf.