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Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle
Crystal structures group II chaperonin reveal closed states associated protein folding cycle
2015/12/11
Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we de...
The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation.
dynamic conformational cycle group I chaperonin C-termini revealed molecular dynamics simulation.
2015/12/11
Chaperonins are large ring shaped oligomers that facilitate protein folding by encapsulation within a central cavity. All chaperonins possess flexible C-termini which protrude from the equatorial doma...