Principal investigator Cees Dekker
E-mail address email@example.com
For more projects, see https://ceesdekkerlab.nl/come-join-us/student-projects/.
A ground-breaking adventure in the fascinating world of pattern formation
Pattern formation is a phenomenon that appears at all biological levels, from pattern-forming proteins used for cell division to the stripes on the animal fur. How do these pattern-forming systems work? To answer this question, we’re not just exploring, but actively creating these captivating phenomena using the power of DNA nanotechnology. Imagine crafting stunning patterns from the simplest of systems!
You will work in a multidisciplinary experimental environment and also in close collaboration with experts in the theory and modelling of pattern formation.
We are looking for an independent, creative, and passionate Master student (starting preferably in January 2024) ready to craft stunning and mesmerising patterns from scratch! Let your curiosity lead the way and join us on this exciting exploration!
- Designing DNA strands
- Testing the system using fluorescence microscopy
- Performing bulk fluorescence measurements
- Understanding the relation between our artificial systems and biological ones
Building a living cell from scratch using microfluidics
Supervisor: Bert van Herck, firstname.lastname@example.org
Throughout the course of evolution life has developed a staggering complexity at the cellular level. To shed light on the fundamental blueprint of a cell and get a better understanding of the governing principles of cellular life, we are aiming to build a synthetic cell from the bottom-up using molecular building blocks (www.basyc.nl).
More specifically, we developed a microfluidic technology, Octanol-assisted Liposome Assembly (OLA), to produce cell-sized (5–20 µm) liposomes in our lab. These liposomes can be immobilized using microfluidic traps for further manipulations. In the past, we already succeeded in mimicking the form of rod-shaped bacteria by squeezing the liposomes into narrow confinements. Further, liposome growth was established by recruiting lipids from the external environment, and liposome division was induced by colliding them against well-defined microfluidic structures. Now the time has come to combine these modules into an integrated lab-on-a-chip system to establish a dynamic cycle of growing and dividing liposomes, mimicking a continuous life cycle of a living cell.
- Microfluidic setup
- Basic light- and epifluorescence microscopy
- On-chip production of synthetic cells
Protein sequencing with nanopores
Supervisor: Justas Ritmejeris, email@example.com
Nanopore technologies have been used by astronauts aboard the International Space Station and biologists travelling across the far reaches of the Earth to study DNA at the single-molecule level. However, analyzing the protein composition of cells at the single-molecule level, while an extremely valuable diagnostic tool, remains a difficult task. In this project we are taking important steps in developing nanopore technologies for proteomics.
Currently, we are exploring methods inspired by nanopore DNA sequencing. This approach involves attaching a small piece of protein (peptide) to a DNA strand to form a peptide-oligo conjugate (POC) which is pulled through a nanopore by a DNA motor enzyme. By measuring the ion current through the pore as the peptide moves through it, we can distinguish individual amino acids and detect important post-translational modifications! Our group has pioneered the proof-of-concept of this method, but engineering and data analysis breakthroughs are needed to push this technology to the next stage!
- Wet lab
- Handling data sets
The ring of power: Building a biomimetic nuclear pore complex with DNA origami
The nuclear pore complex (NPC) is a huge, ring-shaped protein system inserted into the nuclear membrane that allows only certain macromolecules to translocate into the nucleus. It is an incredibly complex system that we aim to study using a bottom-up approach.
Our goal is to build a NPC from scratch by combining different NPC proteins (nucleoporins) grafted inside a ring-like DNA origami structure. This approach gives us precise control over the stoichiometry and the positioning of individual proteins. We utilize this platform to study the arrangement and structural dynamics of the FG-nucleoporins in the pore on the single-molecule level.
- Designing, folding and assembling DNA origami rings
- Protein functionalization of the DNA origami structure
- Gel electrophoresis
- Mass photometry
- Fluorescence correlation spectroscopy
- Fluorescence microscopy
- Transmission electron microscopy