Article
Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate.
Proteins - 1 Jun 2011
Sharma Sandeep K, De Los Rios Paolo, Goloubinoff Pierre
Abstract excerpt
During mild heat-stress, a native thermolabile polypeptide may partially unfold and transiently expose water-avoiding hydrophobic segments that readily tend to associate into a stable misfolded species, rich in intra-molecular non-native beta-sheet structures. When the concentration of the heat-unfolded intermediates is elevated, the exposed hydrophobic segments tend to associate with other molecules into large...
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