A complete understanding of a protein-folding mechanism requires description of the
distribution of microscopic pathways that connect the folded and unfolded states. This …

Highlights•Single molecule FRET experiments determine average transition path
times.•Observed times are extremely close to those found in all-atom MD simulations.•Times …

Although protein-folding studies began several decades ago, it is only recently that the tools
to analyze protein folding at the single-molecule level have been developed. Advances in …

Single‐molecule spectroscopy is an important new approach for studying the intrinsically
heterogeneous process of protein folding. This Review illustrates how different single …

Protein folding is inherently a heterogeneous process because of the very large number of
microscopic pathways that connect the myriad unfolded conformations to the unique …

To obtain quantitative information on the size and dynamics of unfolded proteins we
combined single-molecule lifetime and intensity FRET measurements with molecular …

The folding and dynamics of globular proteins is a multidimensional problem. The structures
of the heterogeneous population of refolding protein molecules are characterized by …

We report single-molecule folding studies of a small, single-domain protein, chymotrypsin
inhibitor 2 (CI2). CI2 is an excellent model system for protein folding studies and has been …

Fluorescence arguably constitutes the most widely used experimental approach in the field
of protein folding. Hence, any review of the use of fluorescence to probe protein stability and …

The folding dynamics of small proteins are often described in terms of a simple two-state
kinetic model. Within this notion, the behavior of individual molecules is expected to be …