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.

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

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

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

The physical interaction network encoded in the multi-domain protein native structure handles the trade-off between the fast, stable folding and the efficient, reliable function.