MPI of Biochemistry, Chaperonin-assisted Protein Folding
Chaperonin-assisted Protein Folding
Am Klopferspitz 18
+49 (89) 8578 - 2204 or - 3759
Fax: +49 (89) 8578 - 2298
The discovery and functional analysis of the chaperonins was instrumental in shaping our present view of de novo protein folding as a chaperone-assisted process. The chaperonins are the paradigm macromolecular machines of protein folding. While many aspects of their ATP-dependent mechanism have been unravelled in the past 15 years, it remains unclear how protein folding inside the chaperonin cage differs from spontaneous folding in bulk solution in terms of the pathways and energetics of the folding reactions. We are addressing these questions using the chaperonin system of E. coli, GroEL and GroES, as our main model. The other major focus of the group involves the mechanism of assembly and activation of hexadecameric form I Ribulose-bisphosphate carboxylase-oxygenase (Rubisco), the abundant enzyme that converts atmospheric CO2 into organic compounds in photosynthesis. With the knowledge we have of the structural functional relationship of Rubisco with its various interacting chaperones, we are using directed evolution to engineer a Rubisco with better catalytic activity.
Primary Techniques: Enzymatic assays, Fluorescence and Single molecule fluorescence spectroscopy, Hydrogen-deuterium exchange mass spectrometry
Model Organisms: Escherichia coli, Chlamydomonas reinhardtii, Arabidopsis thaliana