Many of the synergistic interactions between mutations are modified in the context of unstable proteins in a manner that depends on how the variants promote misfolding in the cell.

An exceedingly low speed limit was estimated for a helical hairpin formation by analyzing hours-long, incessant structural transitions.

How the process of protein folding may be controlled by the Sec machinery to assist protein transport across membranes.

Native state dynamics of mouse prion protein were measured, and these motions were shown to be having a role in initiation of aggregation.

The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.

Adapting a cytosolic enzyme that breaks down glutathione to function in the lumen of the endoplasmic reticulum challenges the long-held view that reduced glutathione fuels disulfide rearrangements during protein folding.

Proteins can fold deeper inside ribosomes with an enlarged exit tunnel.

Development of sequential mixing, single turnover stopped-flow approach reveals processive protein unfolding catalyzed by Escherichia coli ClpB.

The energy landscape of SNARE folding and assembly is optimized for efficient stage-wise membrane fusion.

Identification of Cl⁻-induced folding advances the field’s understanding of prestin’s unique voltage-sensing mechanism and its involvement in mammalian hearing sensation.