** Applications are now closed **
A post-doctoral position is available to develop completely new protein scaffolds and elaborate these into de novo enzymes. This BBSRC-funded post is available for three years. It is in the protein design laboratory of Prof Dek Woolfson (Chemistry and Biochemistry, University of Bristol), and in collaboration with Prof Anthony Green’s protein engineering and biocatalysis group (MIB, University of Manchester). The appointed post-doc would design de novo enzymes based on new alpha-helical barrel proteins using a combination of computational design, protein biochemistry, and directed evolution.
Specifically, the work will develop de novo alpha-helical barrel proteins recently designed by the Woolfson group based on its foregoing peptide assemblies (Science 346, 485-8 (2014)). Unlike most natural peptide assemblies and proteins, these alpha-helical barrel peptides and proteins have solvent-accessible channels running completely through them. These lumens have dimensions accessible to small molecules, and the Woolfson group has shown that they can be modified through rational or computational design to incorporate new functions. Specifically, catalytic activity can be installed into the alpha-helical barrel peptides (Nature Chemistry 8, 837-44 (2016)). The new single-chain alpha-helical barrel proteins open possibilities to extend this work considerably towards the construction of de novo enzymes. The aim of the new project is to design alpha-helical barrel proteins that bind small-molecule substrates and perform catalytic transformations. To realise this potential, this project will be in collaboration with the Green lab (Nature 606, 49-58 (2022)) to bring expertise in biocatalysis, and particularly directed evolution and genetic-code expansion to the project.
Further details and how to apply
Research Associate
Closing date
15 September 2023
For informal enquiries
Please contact: Dek Woolfson