HSP70, or heat shock protein M, ~70,000 is a chaperone molecule intended to aid denaturized proteins undergoing heat shock. When the surrounding environment raises above an unsuitable temperature and proteins begin to lose their quaternary or tertiary structure, HSP70 folds into being. It shepherds proteins mid-way in their confirmation past energy wells in their continuation to the correct lowest energy orientation. Once the temperature lowers back down to a reasonable level again, HSP70 denaturizes and fades into the background again.

When one has a fever, this is the chaperone protein that keeps everything in the body from screeching to a hault. It is an immensely useful supplimentary protein, which is probably why it is one of the most biologically conserved proteins known. Among the mountains of evidence, the wide-spread developmental nature of HSP70 is another bolstering fact for evolutionary theory.

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