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 …

How fast can a protein possibly fold? This question has stimulated experimentalists to seek
fast folding proteins and to engineer them to fold even faster. Proteins folding at or near the …

Protein preparation is a critical step in molecular simulations that consists of refining a
Protein Data Bank (PDB) structure by assigning titration states and optimizing the hydrogen …

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

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 …

A recognized shortcoming in current protein simulations is that most force fields are
parametrized with relatively primitive three-site water models. Since the deficiencies of the …

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

For disordered proteins, the dimensions of the chain are an important property that is
sensitive to environmental conditions. We have used single-molecule Förster resonance …

The yeast prion protein Sup35 is a translation termination factor, whose activity is modulated
by sequestration into a self-perpetuating amyloid. The prion-determining domain, NM …

Upon transfer from strongly denaturing to native conditions, proteins undergo a collapse that
either precedes folding or occurs simultaneously with it. This collapse is similar to the well …