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The unfolding story of a redox chaperone
1Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany. m.mayer@zmbh.uni-heidelberg.de
Abstract:
Oxidative stress, especially in combination with heat stress, poses a life-threatening challenge to many organisms by causing protein misfolding and aggregation. In this issue, Reichmann et al. demonstrate how a destabilized linker region of the bacterial chaperone Hsp33 prevents aggregation of a denatured protein by stabilizing structural elements.
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