MPI für Biochemie, Martinsried | Germany
We investigate molecular chaperone functions in protein folding and assembly. One major focus of the group is the mechanism by which the GroEL/GroES chaperonin of E. coli promotes protein folding. The other is to understand the machinery required for the biogenesis and metabolic maintenance of the photosynthetic enzyme Rubisco, with the long-term goal to engineer the enzyme for improved crop yields and biofuel production.
Keywords: Molecular chaperones / folding / assembly / Rubisco / directed evolution