Description
Efficient recombinant protein purification is pivotal in biological research, predominantly relying on affinity tags. However, complete removal of C-terminal tags is problematic since most endoproteases cut towards the C-terminal end of their recognition sequence. Nonetheless, the additional residues on the recombinant protein from the protease recognition sequence after protein tag removal can be adverse to the proper folding or crystallization of the target protein. Here, we harness the power of de novo computational design to develop sequence-specific proteases tailored for C-terminal tag removal without leaving any residues from the recognition sequence, a challenge unmet by currently used proteases. A FACS-based screening method will be used to select highly efficient de novo proteases. Our preliminary computational results show a gradual improvement of the designed models, which signifies the efficiency of our pipeline. Computational enzyme design is advantageous over conventional directed evolution techniques in developing proteases with customized applications, and our approach will open a new scope for developing proteases for a wide range of applications.Period | 1 Jul 2024 |
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Event title | 31st NAWI DocDay |
Event type | Conference |
Location | Graz, AustriaShow on map |
Degree of Recognition | National |
Fields of Expertise
- Human- & Biotechnology
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Projects
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FWF - ArtEnzDes - Design of Artificial Enzymes for the Baylis-Hillman reaction
Project: Research project