The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. This talk will provide
an overview of new approaches to study and manipulate signaling in living cells and …

Protein folding research stalled for decades because conventional experiments indicated
that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay …

Protein folding is a classic grand challenge that is relevant to numerous human diseases,
such as protein misfolding diseases like Alzheimer's disease. Solving the folding problem …

We combined rapid microfluidic mixing with single-molecule fluorescence resonance energy
transfer to study the folding kinetics of the intrinsically disordered human protein α-synuclein …

Fast-folding proteins have been a major focus of computational and experimental study
because they are accessible to both techniques: they are small and fast enough to be …

In this review, I discuss the various methods researchers use to unfold proteins in the lab in
order to understand protein folding both in vitro and in vivo. The four main techniques …

Protein stability, folding and unfolding rates are all determined by the multidimensional
folding free energy surface, which in turn is dictated by factors such as size, structure, and …

Charged residues on the surface of a protein are known hot-spots for post-translational
modification, protein/ligand-binding, and tuning conformational stabilities. Recent …

The B1 domain of protein G has been a classic model system of folding for decades, the
subject of numerous experimental and computational studies. Most of the experimental work …

For the past two decades, protein folding experiments have been speeding up from the
second or millisecond time scale to the microsecond time scale, and full-atom simulations …