For the final part of my MSc. degree in Applied Physics, I had the pleasure to join the conjoint work between the Chirlmin Joo Lab and Cees Dekker Lab. During my 1-year project, I got to experience single-molecule biophysics; a field I had been interested in for a long time.

The main topic of my research was single-molecule biophysics. Specifically, we tried to characterize individual proteins using nanopores. This measurement method uses nanometer sized pores (or nanopores) to study protein structure by measuring the blockade current due to the protein passing through the pore as a result of the bias voltage (see cover image). Here is a review paper on single-molecule protein sequencing by my supervisor Laura.


One of our main results was the identification of so-called post-translational modifications (ptm), which are essentially tiny chemical add-ons which organisms use as e.g. biomarkers. What makes this important is that we showed for the first time that no extra chemical modifications needed to be applied to these ptms to make them measurable using nanopore sensing. In the end, we were able to distinguish three different variants of a short peptide chain, a non-modified type, a phosphorylated type and a glycosylated type (see image).


We also studied other protein structures and tried to observe unfolding of proteins through a nanopore, as well as studying the nanopore itself in more detail. You can find my full MSc. Thesis report here (40MB). Part of this work was published in ACS Nanoletters (2019).