Hendrik Grallert

Learn More
The GroE chaperone system consists of two ring-shaped oligomeric components whose association creates different functional states. The most remarkable property of the GroE system is the ability to fold proteins under conditions where spontaneous folding cannot occur. To achieve this, a fully functional system consisting of GroEL, the cochaperone GroES, and(More)
The GroE chaperones of Escherichia coli promote the folding of other proteins under conditions where no spontaneous folding occurs. One requirement for this reaction is the trapping of the nonnative protein inside the chaperone complex. Encapsulation may be important to prevent unfavorable intermolecular interactions during folding. We show here that,(More)
Many data sources on the Web evolve: they change their content over time, typically as reactions to events. Such changes often need to be mirrored in data on other Web nodes: updates need to be propagated. To respond to the need for evolution and reactivity both locally and globally, the language XChange has been developed. We demonstrate its applicability(More)
The prokaryotic molecular chaperone GroE is increasingly expressed under heat shock conditions. GroE protects cells by preventing the irreversible aggregation of thermally unfolding proteins. Here, the interaction of GroE with thermally unfolding citrate synthase (CS) was dissected into several steps that occur before irreversible aggregation, and the(More)
This report presents the refinements made in the prototypes described in the previous deliv-erable (deliverable I5-D5 – " A first prototype on evolution and behaviour at the XML level "), and their usage in use-case scenarios. In particular, the use-case scenarios have been chosen according to the sketch of use-cases designed in the deliverable I5-D2&3 – "(More)
The molecular chaperones GroEL and GroES facilitate protein folding in an ATP-dependent manner under conditions where no spontaneous folding occurs. It has remained unknown whether GroE achieves this by a passive sequestration of protein inside the GroE cavity or by changing the folding pathway of a protein. Here we used citrate synthase, a well studied(More)
  • 1