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Foto Research workgroup Schacherl

Structural Enzymology (Schacherl lab)

The Schacherl lab investigates molecular mechanisms and three-dimensional structures of eukaryotic proteins and their complexes using biophysical methods across different scales.

The following fundamental questions are investigated:

  • How do enzymes recognize their substrates and how are they regulated?
  • How are protein (complexes) and enzymes organized in situ?
  • How can disease-relevant variants be restored using nanobodies?

 

 

 

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Research Group Structural Enzymology

The main focus of the Schacherl group is the investigation of structure-function relationships and the dynamics of human protein complexes and enzymes. For this purpose, the group uses various biochemical, biophysical and structural biological methods, such as three-dimensional cryo-electron microscopy and tomography, as well as crystallography.

The main protein targets are proteases and guanylate cyclases, which perform various functions in the cell and play crucial roles in diverse human diseases. Another focus is on the analysis and interpretation of macromolecular machines, such as the ribosome. In addition, the group selects and uses nanobodies to study protein structures and as potential therapeutics in the future.

The Schacherl group is currently establishing and using correlative cryo-light and electron microsopic workflow to study the organization of protein (complexes) and enzymes in situ (inside the cell). This involves working with primary cells and established laboratory cell cultures.

The Schacherl group is open to collaborations with non-structural biologists who would like to study their target proteins individually at atomic resolution or in a cellular context at subatomic resolution.

 

Methods

A variety of biochemical and biophysical methods are used within the research group. These include the following:

  • Cryo-electron microscopy (SPA/single particle analysis).
  • Correlative cryo-light and electron microsopic workflow (cryo-CLEM/ET)
  • Crystallization of proteins and macromolecular crystallography
  • Development of specific nanobodies using in vitro selection methods
  • Heterologous protein expression in bacteria, insect and human cell lines
  • Isolation of proteins from native tissues
  • Site-directed mutagenesis
  • Chemical crosslinking
  • Fluorescence spectroscopy and fluorescence anisotropy
  • Surface Plasmon Resonance (SPR)