Atp

The released protein is fully folded or in a partially folded state that is committed to adopt the native conformation.

Protein folds inside the enclosure.

7 ATP and GroES bind to GroEL with a filled pocket.

FIGURE 4-31 Chaperonins in protein folding. (a) A proposed pathway for the action of the E. coli chaperonins GroEL (a member of the Hsp60 protein family) and GroES. Each GroEL complex consists of two large pockets formed by two heptameric rings (each subunit Mr 57,000). GroES, also a heptamer (subunits Mr 10,000), blocks one of the GroEL pockets. (b) Surface and cut-away images of the GroEL/GroES complex (PDB ID 1AON). The cut-away (right) illustrates the large interior space within which other proteins are bound.

7 ATP and GroES bind to GroEL with a filled pocket.

diates with inappropriate disulfide cross-links. Peptide prolyl cis-trans isomerase (PPI) catalyzes the interconversion of the cis and trans isomers of Pro peptide bonds (Fig. 4-8b), which can be a slow step in the folding of proteins that contain some Pro residue pep-tide bonds in the cis conformation.

Protein folding is likely to be a more complex process in the densely packed cellular environment than in the test tube. More classes of proteins that facilitate protein folding may be discovered as the biochemical dissection of the folding process continues.

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