Description
We propose to computationally design novel ligand binding and catalytically active proteins by harnessing the high thermodynamic stability of de novo helical proteins.
We aim to:
-Characterize to which extent we can harness the stability of parametrically designed helical bundles to introduce deviations from ideal geometry.
-Develop a new computational design strategy, which expands on the Crick coiled-coil parametrization and allows to rationally build non-ideal helical protein backbones at specified regions in the desired structure.
-Investigate new strategies to design the first cascade reactions into de novo designs.
We aim to:
-Characterize to which extent we can harness the stability of parametrically designed helical bundles to introduce deviations from ideal geometry.
-Develop a new computational design strategy, which expands on the Crick coiled-coil parametrization and allows to rationally build non-ideal helical protein backbones at specified regions in the desired structure.
-Investigate new strategies to design the first cascade reactions into de novo designs.
| Status | Active |
|---|---|
| Effective start/end date | 1/04/19 → 31/03/24 |