“…It is well accepted that a flexible dynamic quaternary structure is necessary for sHSPs activity [ 1 , 4 , 10 , 28 ]. Changes in the cellular environment, such as temperature [ 9 , 10 , 27 , 29 ], pH [ 30 ], the presence of ions [ 31 , 32 ], post-translational modification (phosphorylation) [ 33 , 34 , 35 ], redox environment [ 7 , 30 ] and crowding [ 19 , 25 , 32 , 36 , 37 , 38 ] also regulate chaperone activity by affecting the structural and oligomerization dynamics of sHSPs [ 4 , 5 ]. It has been reported that sHSP dynamics is a very complex process that includes five levels of regulation: (1) flexible domains flanking the ACD, (2) polydisperse self-oligomerization, (3) hetero- oligomerization with other sHSPs, (4) subunit exchange, and (5) regulation by the cellular environment [ 5 , 39 ].…”