title: The unfolding story of a redox chaperone.
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.
authors.affiliation: Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany. m.mayer@zmbh.uni-heidelberg.de
authors.forename: Matthias P
authors.initials: MP
authors.lastname: Mayer