The chaperonin GroEL assists protein folding through ATP-dependent, cooperative movements that alternately create folding chambers in its two rings. The substitution E461K at the interface between ...

All chaperonins mediate ATP-dependent polypeptide folding by confining substrates within a central chamber. Intriguingly, the eukaryotic chaperonin TRiC (also called CCT) uses a built-in lid to close ...

Without ATP, the chamber is open. When ATP is added, the chamber closes. "The take home message in this is how the chaperonin opens and closes," said Chiu. The way in which these chaperonins complete ...

Using the exceptionally bright and powerful X-ray beams of the Advanced Light Source, researchers have discovered a critical control element within chaperonin, the protein complex responsible for the ...

Cryo-electron tomography (cryo-ET), can be used to visualize and analyze cellular structures in their natural environment. Researchers at the MPI of Biochemistry in Martinsried and the University ...

In a new study in archaea (single-celled organisms without nuclei to enclose their genetic information), researchers have discovered how the Group II chaperonins close and open folding chambers to ...

Cryo-electron tomography, or cryo-ET for short, can be used to visualize and analyze cellular structures in their natural environment. Researchers at the Max Planck Institute of Biochemistry (MPIB) in ...