Laura M Chamness, Charles P Kuntz ... Jonathan P Schlebach
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.
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.
Xiaoxuan Lin, Patrick R Haller ... Tobin R Sosnick
Identification of Cl−-induced folding advances the field’s understanding of prestin’s unique voltage-sensing mechanism and its involvement in mammalian hearing sensation.
Alexander Borodavka, Eric C Dykeman ... Don C Lamb
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.