The properties of unfolded proteins have long been of interest because of their importance
to the protein folding process. Recently, the surprising prevalence of unstructured regions or …

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 …

Single-molecule spectroscopy has developed into an important method for probing protein
structure and dynamics, especially in structurally heterogeneous systems. A broad range of …

The successful incorporation of enzymes into materials through multipoint covalent
immobilization (MPCI) has served as the foundation for numerous advances in diverse …

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 …

The dynamics of proteins in solution includes a variety of processes, such as backbone and
side-chain fluctuations, interdomain motions, as well as global rotational and translational …

As nanometer-scale portals in biological membranes, protein ionic channels act as
gatekeepers, controlling the traffic of ions and macromolecules into and out of cells …

We use the statistics of photon emission from single molecules to probe the ultrafast
dynamics of an unfolded protein via Förster resonance energy transfer. Global …