Proteins are increasingly used in basic and applied biomedical research. Many proteins,
however, are only marginally stable and can be expressed in limited amounts, thus …

The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in
an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with …

Mutations in a protein active site can lead to dramatic and useful changes in protein activity.
The active site, however, is sensitive to mutations due to a high density of molecular …

We recently reported on small-molecule inhibitors of the GroES/GroEL chaperone system as
potential antibiotics against Escherichia coli and the ESKAPE pathogens but were unable to …

Recent years have seen a dramatic improvement in protein-design methodology.
Nevertheless, most methods demand expert intervention, limiting their widespread adoption …

Computational simulations of protein folding can be used to interpret experimental folding
results, to design new folding experiments, and to test the effects of mutations and small …

Fluorescent protein (FP) maturation can limit the accuracy with which dynamic intracellular
processes are captured and reduce the in vivo brightness of a given FP in fast-dividing cells …

Chaperonins are biological nanomachines that help newly translated proteins to fold by
rescuing them from kinetically trapped misfolded states. Protein folding assistance by the …

Confining compartments are ubiquitous in biology, but there have been few experimental
studies on the thermodynamics of protein folding in such environments. Recently, we …

Förster resonance energy transfer (FRET)-based sensors are a valuable tool to quantify
cell biology, yet it remains necessary to identify and prevent potential artifacts in order to …