Properly folded protein

Properly folded protein

GroEL "tight" conformation

GroEL "relaxed" conformation

▲ FIGURE 3-11 Chaperone- and chaperonin-mediated protein folding. (a) Many proteins fold into their proper three-dimensional structures with the assistance of Hsp70-like proteins (top). These molecular chaperones transiently bind to a nascent polypeptide as it emerges from a ribosome. Proper folding of other proteins (bottom) depends on chaperonins such as the prokaryotic GroEL, a hollow, barrel-shaped complex of 14 identical 60,000-MW subunits arranged in two stacked rings.

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