During and following translation proteins can be modified in highly diverse ways. A very frequently occurring protein modification in (higher) eukaryotes is the acetylation of a protein’s amino terminus (N-terminus).
While this modification changes the biophysical parameters of this N-terminus, surprisingly little is known about the functional consequences, if any, of this modification for the grand majority of acetylated proteins.
Recent studies indicated the possibility that an N-terminal acetyl group can affect protein folding and thus protein conformation.
In this project, we will improve a mass spectrometry-based method for assessing protein conformation on a cellular scale.
This method will then be applied to the proteomes of human cell lines that are models for human diseases. Selected proteins with altered conformation will be further validated using other molecular technologies by which we hope to get more insights into protein folding diseases, amongst others.
Our aim is thus to evaluate the absence or reduction of N-terminal acetylation on a proteome’s conformation.
Desirable but not required
Experience with cloning is desired.
Key personal characteristics
We will hire an enthusiastic, warm and motivated young scientist who considers science as her / his playground! You should have a keen interest in proteomics, good communication and writing skills (English), and should be able to work independently, as well as function as part of a team.
We offer a position for two times two years. The candidate will work in a stimulating multicultural environment in the proteomics lab of Prof.
Dr. Kris Gevaert. She / he will have access to cutting-edge technologies, personal career assistance and high-level training courses.
The position is immediately available.
How to apply?
Note that additional information can be given per e-mail request to Kris Gevaert ().