GroEL is a cylinder-shaped molecule, made of two rings stacked back to back. A key partner in its function is GroES, a ring-shaped "co-chaperonin" that binds to each end of GroEL like a domed lid.

GroEL is alternately bound and unbound by a co-chaperonin, GroES. Against expectations, the 'football' complex -- where two GroES units cap the cylindrical GroEL at either end ...

The chaperonin GroEL binds folding intermediates of four-disulfidehen lysozyme transiently within its central cavity. Using stopped flow fluorescence we show that GroEL binds early intermediates ...

GroEL binds the PA prepore. Incubating GroEL with the PA prepore at pH 8.5, a condition under which the prepore-to-pore transition is not observed, gave rise to a single band that migrated above ...