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| Name |
Hartl, F. Ulrich |
| Location
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Max Planck Institute of Biochemistry |
| Primary Field
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Biochemistry |
 Election Citation
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Hartl is a pioneer of the protein folding field. Hartl was the first to show that chaperones assist the folding of polypeptide chains in vivo, reconstituted the pathway of chaperone-assisted folding in vitro, and discovered that protein folding takes place in the cavity of the GroEL chaperonin, a key insight.
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Research Interests
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Research in the Hartl laboratory focuses on the mechanisms of protein folding and quality control in the cell. Our goal is to reach a comprehensive understanding, at the structural and functional level, of how the machinery of molecular chaperones assists folding through the cooperation of co- and post-translational mechanisms. A long-standing interest is to understand how the cylindrical chaperonins of the GroEL type promote and modulate the folding process. Our second major research focus concerns the molecular mechanisms of proteotoxicity in diseases associated with protein misfolding and aggregation, including Parkinson's, Alzheimer's and Huntington's diseases. Here we wish to understand how the cellular machinery of protein homeostasis (proteostasis) normally provides protection and why these defense mechanisms increasingly fail during aging, facilitating the manifestation of neurodegeneration. We are using a wide range of methods from cellular biochemistry, biophysics and structural biology. In understanding the proteostasis network we are increasingly using systems-based approaches, including quantitative proteomics and genetic screens.
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