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Protein folding is the transformation of a linear amino acid sequence in the unique three dimensional structure of a protein. This process is fundamental to life. Understanding the underlying principles of protein folding is one the most daunting open questions in biochemistry. Folding is a spontaneous process. In the living cell, a complex, ATP-driven machinery of proteins exists which assists the structure formation process.
What are the big open questions and how are we going to solve them? We would like to know how molecular chaperones work. How do they process their client proteins? How is the energy of ATP transformed into conformational changes? What are the sets of client proteins for the different chaperones? How do co-chaperones affect the mechanism of the respective partner chaperone?
To answer the above questions, we apply a range of techniques, from molecular biology to biochemistry/biophysics to cell biology. Ideally, in vitro and in vivo approaches are combined to achieve a multi-facetted view of how these ATP-driven machines work. In addition, we try to get insight into the spontaneous folding of proteins with a view to define intermediates and to establish folding protocols for proteins of biotechnological interest.
- Haslbeck, M. et al. (2004). Hsp42 is the general
small heat shock protein in the cytosol of Saccharomyces
cerevisiae. EMBO J. 23, 638-649.
- Buchner, J. & Kiefhaber, T. (2005).
Protein Folding Handbook. Wiley-VCH, Weinheim.
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