In this review, we discuss the potential of molecular chaperones belonging to GroEL family as applied to different practical uses. The GroEL, often referred to as chaperonin, plays a fundamental role in protein folding in cells and is essential for the proper folding of a number of proteins. Early on in studying chaperones it has been considered, along with other chaperones, as an attractive tool to assist recombinant protein folding in cells and their refolding in vitro. Several different schemes for using GroEL have been applied for difficult-todeal with recombinant targets, especially those insoluble and unstable. Fusion constructs of difficult recombinant targets with GroEL as a carrier have been reported to make them better soluble. However, the complex structure of GroEL particle, consisting of two hexamer rings, often makes it difficult to take full advantage of its use as a versatile (re)folding tool. Subsequently, a separately expressed GroEL apical domain, minichaperone, was not only extensively studied as representative of the substrate-binding site of the full-sized GroEL, but also used as an aiding tool for refolding of recombinant proteins in different settings. In separate venues of research, immune-modulating activity of chaperonins has been studied. Mycobacterial GroEL has been used as an immune-stimulating carrier to make therapeutic vaccines. In spite of the progress made, to really meet all the expectations for GroELs, minichaperone and other chaperonin forms, bioengineering and further crafting is required to make them truly useful nano tools for specific applications.”

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