Positions

Design nanopores

One of the main challenges in protein chemistry is the ability of designing proteins with a target structure and function. In the collaboration with the molecular dynamic group at the University of Groningen we are aiming of using advanced chemical and biochemical techniques to  design nanopores and artificial transmembrane proteins.
The aim is to design an artifical protocell bottin-up, and to provide next-generation naopore sensors for single-molecule analysis.

Position: PhD or PostDoc
Background: Protein chemistry, MD simulation, Biochemistry
Sponsor: ERC

Proteins adaptor for single-molecule sensing

We have recently shown that proteins can be internalised inside a ClyA nanopore and the binding of ligands to the protein can be measured. Crucially the nanopore system can identify and quantify the ligand directly in blood or sweat.

The project has two aims: 1)  The identification of several proteins that can be internalised inside the nanopore 2) The modulation of the binding affinity of the internalised protein to recogne the ligand at physiological ligand concentrations.  

Single-molecule protein sequencing

The large-scale study of the proteins produced by an organism, proteomics, is crucial in order to understand cellular processes underlining diseases and to identify specific indicators linked to diseases.  

This project aims to develop a new platform for protein sequencing using  nanopores. This will be the first technology that will be able to identify and sequence proteins at the single-molecule level.

More in details, the candidate is part of a consortium that includes researchers from Delft and Wageningen, and will develop, engineer and re-design biological nanopores that will allow the sequence identifications of proteins as they are translocated across a nanopore

Position: PhD or PostDoc
Background: Chemistry, Biochemistry or Biophysics
Sponsor: ERC

Single molecule enzymology

Unraveling the role of protein dynamics play and understanding how proteins can fold are among the last remaining grand challenges in enzymology. We are aiming at using biological nanopores to sample the conformational dynamic of individual native proteins and the folding unfolding of proteins at the single molecule level.

The candidate will study important enzymatic reactions such as the dihydrofolate reductase or the adenylate kinase to underpin the importance of conformational dynamics in enzymatic reactions.

Further, the protein will be immobilized inside the lumen of the nanopore and the folding-unfolding of the protein will be monitored by nanopore currents.

Background: Chemistry, Biochemistry, biotechnology, Enzymology