GroEL and GroES are E.coli chaperones, which are homologs of the mitochondrial chaperones Hsp60 and Hsp10 respectively. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding in an ATP-dependent mechanism. Binding of substrate protein, in addition to binding of ATP, induces a conformational change that allows association of this binary complex with a separate lid structure, GroES.
has not yet been referenced specifically in any publications.
Publishing research using ab73737? Please let us know so that we can cite the reference in this datasheet.
Customer reviews and Q&As
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
Get resources and offers direct to your inboxSign up