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.