Förster resonance energy transfer (FRET) in association with the recent advancements in
optical techniques provides a way to understand the detailed mechanisms in different …

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

Unfolded states of proteins and native states of intrinsically disordered proteins (IDPs)
populate heterogeneous conformational ensembles in solution. The average sizes of these …

Protein stability often is studied in vitro through the use of urea and guanidinium chloride,
chemical cosolvents that disrupt protein native structure. Much controversy still surrounds …

Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

Single-molecule FRET (smFRET) has become a mainstream technique for studying
biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by …

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 …

Transition paths are a uniquely single-molecule property not yet observed for any molecular
process in solution. The duration of transition paths is the tiny fraction of the time in an …

We used single-molecule FRET in combination with other biophysical methods and
molecular simulations to investigate the effect of temperature on the dimensions of unfolded …

Chemical denaturants are the most commonly used agents for unfolding proteins and are
thought to act by better solvating the unfolded state. Improved solvation is expected to lead …