User:Ten Topgyal/sandbox

Chaperone holdases: most ATPindependent chaperones work as chaperone holdases. They tightly bind to unfolding client proteins and prevent their aggregation. Some chaperone holdases are specifically active under distinct stress conditions (e.g., Hsp33), whereas others, such as Hsp40, are constantly active under normal conditions. Stress-activated chaperone holdases often depend on ATP-dependent foldases for client refolding once stress conditions subside. The recently discovered bacterial chaperones Spy and HdeA, which reside in the bacterial periplasm, show both ATPindependent holdase and foldase functions.