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 …

The dimensions of unfolded and intrinsically disordered proteins are highly dependent on
their amino acid composition and solution conditions, especially salt and denaturant …

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

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

Interactions between the synaptic protein α-Synuclein and cellular membranes may be
relevant both to its native function as well as its role in Parkinson's disease. We use single …

Studying the conformational landscape of intrinsically disordered and partially folded
proteins is challenging and only accessible to a few solution state techniques, such as …

The aggregation and deposition of normally soluble proteins is the hallmark of several
devastating neurodegenerative disorders. For proteins such as tau in Alzheimer's disease …

We have used the combination of single-molecule Förster resonance energy transfer and
kinetic synchrotron radiation circular dichroism experiments to probe the conformational …

Intrinsically disordered proteins (IDPs) are increasingly recognized for their important roles
in a range of biological contexts, both in normal physiological function and in a variety of …