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Chaperonins Prompt Proper Protein Folding -- But How?

In proper society of yesterday, a chaperone ensured that couples maintained appropriate courting rituals. In biology, a group of proteins called chaperonins make sure that proteins are folded properly to carry out their assigned roles in the cells.

In a new study in archaea (single-celled organisms without nuclei to enclose their genetic information), a consortium of researchers from Baylor College of Medicine and Stanford University in California discovered how the Group II chaperonins close and open folding chambers to initate the folding event and to release the functional protein to the cell. A report of their work appears in the current issue of the journal Nature.

Archaea is one of three major divisions in the classification of living organisms. The other two are bacteria and eukaryotes. Archaea lack a nucleus but have other characteristics that are similar to those of eukaryotes, which include human beings.
 
 

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