Protein folding studied by single-molecule FRET.

By Benjamin Schuler, W. Eaton. Current Opinion in Structural Biology, 2008

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Dynamics of proteins in solution (2019, background): “Labeling two sites on a single molecule, folding dynamics under native and denaturing conditions can be studied (Nienhaus, 2006; Borgia et al., 2008; Schuler and Eaton, 2008; Ferreon and Deniz, 2011).”
Learning rates and states from biophysical time series: a Bayesian approach to model selection and single-molecule FRET data. (2009, background): “FRET (10, 11, 12, 13) refers to the transfer of energy from a donor fluorophore (which has been excited by short-wavelength light) to an acceptor fluorophore (which then emits light of a longer wavelength) with an efficiency which decreases as the distance between the fluorophores increases.”
A practical guide to single-molecule FRET (2008, background): “FRET measurement of freely diffusing single molecules is simpler to implement (commercial solutions are also available: for example, MicroTime200 from PicoQuant ) and is powerful in revealing population distributions of inter-dye distance”
A BIRD’S EYE VIEW: TRACKING SLOW NANOMETER-SCALE MOVEMENTS OF SINGLE MOLECULAR NANO-ASSEMBLIES (2010, positive): “Fluorescence-based tools are now being employed to understand the properties and dynamics of proteins (Giepmans et al., 2006; Min et al., 2005; Schuler and Eaton, 2008; Shi et al., 2008) and nucleic acids (Ditzler et al., 2007; Joo et al., 2008; Pljevaljcic and Millar, 2008; Zhao and Rueda, 2009).”