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The chaperonins are a family of barrel shaped cellular components with a flap or lid like closure mechanism located in the cell nucleus. There are many different families of chaperones. Each family acts to aid protein folding in a different way. After some unformed proteins are extruded from the ribosome, they are transported by molecular machines to the chaperones. After the chaperones admit the newly formed proteins, a linear chain of amino acids, they perform the duty of folding and refolding them into specific and more functional three-dimensional shapes. Some classes also re-fold proteins damaged by cellular stressors such as infection, inflammation, exposure to cellular toxins, starvation, water deprivation etc. More recently, it has been discovered that chaperonins may have the additional property of acting as cell-to-cell signaling molecules and this function is under study to uncover more details.

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