Crystal Structure of Escherichia coli GroEL in Substrate and ADP Unloaded State

Stability of the chaperonin system GroEL–GroES under extreme environmental conditions

“…24,50,51 K + and Mg 2+ ions play also an important role for ATP binding and hydrolysis and have an impact on the stability of GroEL. [52][53][54] Temperature-induced unfolding of proteins is mainly driven by the conformational entropy gain of the peptide chain, whereas the overall volume change plays the decisive role in the pressure-induced unfolding scenario. 16,41 The system tends to occupy a smaller volume state at high pressure, which includes the filling and elimination of internal void volume and cavities as possible mechanism for pressure-induced unfolding.…”