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In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediatethe folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participatein all these processes through their ability to recognize nonnative conformations of other proteins. They bindextended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membranetranslocation, or following stress-induced damage
