Publisher Summary This chapter describes several experiments that give a qualitative feel
for how Type II chaperonins might facilitate protein folding. Imaging of CCT/actin complexes
and experiments on actin and tubulin folding in vitro suggest that target proteins bind to
chaperonin in a surprisingly native-like state, probably consisting of only one or a few
kinetically trapped folding intermediates. Chaperonins are a specialized but ubiquitous
group of molecular chaperones that are characterized by a multisubunit ring structure …