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 shepherd
s 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.