Switiching via common structural framework

Josh explores [ http://www.thinkgene.com/researchers-reveal-insights-into-hidden-world-of-protein-folding/ ] an article from Booth et al. titled 'Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT' [ http://www.nature.com/nsmb/journal/v15/n7/abs/nsmb.1436.html or http://www.scribd.com/doc/3321492/Mechanism-of-lid-closure-in-the-eukaryotic-chaperonin-TRiCCCT ].

clipped from www.thinkgene.com Virtually all proteins have to be folded-some in complex configurations-in order to function properly, and many are known to require a molecule called a chaperone to fold them. Frydman estimates that perhaps 10 percent of the proteins needing chaperones must have one that, like TRiC, is part of the subset called chaperonins. Other work done in Frydman’s lab has shown that proteins that have very complex folds seem to require chaperonins.