Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 32, Issue -, Pages 617-621Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0320617
Keywords
ATP hydrolysis; binding; chaperone; DnaJ protein; Hsp70; substrate recognition
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The role of Hsp70 (heat-shock protein 70) chaperones in assisting protein-folding processes relies on their ability to associate with short peptide stretches of protein substrates in a transient and ATP-controlled manner. In the present study, we review the molecular details of the mechanism behind substrate recognition by Hsp70 proteins.
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