Protein stability in the cage formed by the chaperonin GroEL and its cofactor GroES is reduced by more than 5 kcal mol-1 relative to that in bulk solution.
Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.
Lab-evolved 'super Spy' chaperones show enhanced flexibility, which allows them to bind to and stabilize proteins more effectively than natural chaperones.
Cell-based high-throughput screening identifies IBT21 as a chemical chaperone, that inhibits ER protein aggregation and prevents the cell death caused by a proteotoxin, the aggregation-prone prion protein.
FERONIA receptor kinase interacts with phosphatidylinositol-anchored proteins LORELEI and LLG1 to ensure its proper functional location in the cell membrane and engages them as co-receptors on the cell surface to mediate a broad spectrum of growth and signaling processes.
SatS of Mycobacterium tuberculosis is a new protein export chaperone with a role in exporting proteins by the specialized SecA2 pathway and a role in intracellular growth in macrophages.
Cytosolic and organellar Hsp90s from higher eukaryotes have evolved a variable, and environmentally responsive N-terminal extension to regulate their activity.
NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.