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<p><a href="page.php?w=oligomer">oligomer</a> of between six and eight identical subunits, while the 60 kDa chaperonin (cpn60, or groEL in bacteria) forms a <a href="page.php?w=secondary_structure">structure</a> comprising 2 stacked rings, each ring containing 7 identical <a href="page.php?w=protein_subunit">subunits</a>. These ring structures assemble by self-stimulation in the presence of Mg<sup>2+</sup>-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides an isolated environment for <a href="page.php?w=protein_folding">protein folding</a></p><p>
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