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Hub-proteins that engage in multiple mutually exclusive transient interactions have on average a higher degree of disorder than other proteins [1].This also applies to molecular chaperones,which bind to a large variety of different protein folding intermediates to prevent their non-specific aggregation and facilitate protein folding both in vitro and in vivo.An example is provided by Heat shock protein 60kDa (Hsp60), a chaperone that assists the correct folding of other mitochondrial proteins.Despite the plethora of studies on the mechanism of Hsp60s function, especially in prokaryotes, fundamental issues still remain unexplored.