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Updated: Aug 4, 2026

Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Molecular chaperones: structure of a protein disaggregase
11ZMBH, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120, Heidelberg, Germany. a.mogk@zmbh.uni-heidelberg.de
Abstract:
The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.
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