Research
In the focus of our research are enzymes,
which are elaborate proteins that catalyse cellular reactions with high
specificity and efficiency.
Projects
We are using rational
design and directed evolution to engineer the stability and catalytic activity of
enzymes, experimentally reconstruct the natural evolution of
enzymes, assign
functions to uncharacterised enzymes, and characterize
allosteric interactions within multi-enzyme
complexes. To this end, we apply a broad range of experimental and computational methods.
Model system
Our preferred model system is the (ba)8-barrel
family of enzymes, which is the most frequently encountered
protein fold. (ba)8-barrel
enzymes catalyse a large variety of mechanistically diverse
reactions. The fold of the canonical (ba)8-barrel
consists of a central barrel of eight parallel
b-strands,
which are surrounded by eight external
a-helices.
Connecting loops are located at both the N-terminal (a-b
loops) and the C-terminal (b-a
loops) face of the barrel. Due to the spatial
separation of structural elements that are important for
stability and catalytic activity,
(ba)8-barrels
provide an ideal scaffold
for the study of enzyme evolution and the design of new
enzymatic activities.
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The
(ba)8-barrel fold
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Publications of BC II |
Pubmed Entries: |
R. Sterner
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R. Merkl
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P. Babinger |
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