Editing Biostasis (section)

==== Protein chaperoning ====
In molecular biology, [[Chaperone (protein)|molecular chaperones]] are proteins that assist in the folding, unfolding, assembly, or disassembly of other [[Macromolecule|macromolecular]] structures. Under typical conditions, [[Chaperone (protein)|molecular chaperones]] facilitate changes in shape ([[conformational change]]) of [[macromolecule]]s in response to changes in environmental factors like [[temperature]], [[pH]], and [[voltage]]. By reducing conformational flexibility, scientists can constrain the function of certain proteins.<ref name=":2" /> Recent research has shown that proteins are promiscuous, or able to do jobs in addition to the ones they evolved to carry out.<ref name=":3">{{Cite news|url=https://www.sciencealert.com/the-apromiscuousa-protein|title=The 'Promiscuous' Protein|last=University|first=Massey|work=ScienceAlert|access-date=2018-05-26|language=en-gb}}</ref> Additionally, protein promiscuity plays a key role in the adaptation of species to new environments.<ref name=":3" /> It is possible that finding a way to control [[conformational change]] in promiscuous proteins could allow scientists to induce biostasis in living organisms.<ref name=":2" />