ABSTRACT
Heat Shock Proteins (HSPs) or chaperones are the members of a protein family which act in different stages of protein folding, they protect damaged proteins and prevent them from aggregation and they assist at refolding. As Heat Shock Proteins (HSPs) generally play a key role in the stress response of cells, it might be expected that HSPs are also activated at stress conditions imposed by elevated pressure. Whereas higher order structure of proteins is affected only in the pressure region above 100 MPa cell life is already perturbed in the lower pressure region. It is known that high continuous hydrostatic pressure inhibits protein synthesis in general. Small HSPs (sHSPs) constitute the most variable family of molecular chaperones, they can be found in all kingdoms of life. The possible main role of the sHSPs is to prevent the aggregation of unfolded substrate proteins, and maintain them in a folding-competent state.
