Scientists have studied molecular interactions in the chaperonin protein GroEL. GroEL is alternately bound and unbound by a co-chaperonin, GroES. Against expectations, the 'football' complex -- where ...

Scientists have revealed that the bacterial chaperonin GroEL, with its partner GroES, can capture and refold nascent proteins while they are still being made on ribosomes. This cotranslational folding ...

Kanazawa - Proteins must fold in a specific way to function. This is often assisted by molecular chaperones--small proteins whose job is to help others fold to the right shape. Now, Japanese ...