The periplasm of Gram-negative bacteria is an unusual compartment in that it is very much a part of the cell, yet relatively unshielded from changes in the extracellular environment. The ionic environment within the periplasm closely reflects that of the outside due to the steady flux of ions across the outer membrane. It is within this low energy and volatile space that a suite of chaperones operate to transport, fold, and protect outer membrane and periplasmic resident proteins. This work looks at the unfolded protein response of the periplasm under pH stress and begins to tease apart the relative importance of various chaperones in mitigating this response.