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Chemical Chaperones The term ‘molecular chaperone’ was originally used to describe the function of nucleoplasmin, a nuclear protein that ensures correct assembly of nucleosomes from DNA and histones. Subsequently, the meaning of the term was extended to include a class of structurally unrelated proteins which mediate correct folding of other proteins but do not themselves form a part of the final structure. In a broader sense, they help determine the fate of a protein in the cell. Not only do they ensure correct folding, but also the correct assembly of the units of an oligomeric protein and transport of a protein to its particular subcellular compartment. During heat stress they assume the responsibility of quality control. They bind the heat denatured proteins and catalyze their renaturation.
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