The principles governing the regulation of small heat shock proteins (sHsps) are still not clear. A key feature of the sHsps is the ability to form highly dynamic oligomer structures. To transfer the ATP-independent sHsps in an active conformation, mainly a shift of oligomer size towards smaller species is needed. In the present study, three different triggers to shift the oligomer equilibrium were investigated in detail: the formation of hetero-oligomers, the influence of the N-terminal region, and the effects of the potential co-chaperone Bag3.
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The principles governing the regulation of small heat shock proteins (sHsps) are still not clear. A key feature of the sHsps is the ability to form highly dynamic oligomer structures. To transfer the ATP-independent sHsps in an active conformation, mainly a shift of oligomer size towards smaller species is needed. In the present study, three different triggers to shift the oligomer equilibrium were investigated in detail: the formation of hetero-oligomers, the influence of the N-terminal region,...
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