WCC 27 |
| The prokaryotic chaperonin GroEL consists of two back-to-back stacked homo-heptameric rings with a cavity at each end where protein folding can take place under confining conditions. It is a molecular machine that assists protein folding by undergoing concerted ATP-induced allosteric transitions between protein substrate binding and release states. By contrast, the eukaryotic chaperonin CCT consists of two back-to-back stacked hetero-octameric rings that undergo sequential ATP-promoted allosteric transitions. Evidence will be presented showing that concerted allosteric transitions favor all-or-none protein substrate release and folding whereas sequential transitions result in domain-by-domain substrate release and folding. |
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From Peptide Bond Formation to Functional Proteins: Symposium in Honor of Ada Yonath
8:15 AM-11:10 AM, Tuesday, August 21, 2007 Sheraton Boston -- Back Bay Blrm B, Oral
Women Chemists Committee |