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Welcome to the website of the Arnold Boersma Lab.

We are located in the Cellular Protein Chemistry section at the Bijvoet Centre for Biomolecular Research at Utrecht University in The Netherlands.

We are also associated with the DWI-Leibniz Institute for Interactive Materials in Aachen, Germany.

The Boersma group works in the area of biochemistry, biophysics, chemical biology, and microfluidics.

We aim to determine the causes and consequences of macromolecular crowding. Cells are dense with proteins, DNA, and RNA; these biomacromolecules continuously interact in a Brownian storm through steric and associative or repulsive interactions. On pure steric grounds, one would expect crowding to reduce the volume of a given protein or protein assembly (in most cases). However, the cell is obviously not a box of marbles: So how are all these biomacromolecules organized, and how does this affect the macromolecular crowding effects? Which proteins are involved, and which macromolecules could change shape and function? Is macromolecular crowding essential for living cells? Should we take them into account when considering disease? How does it affect disease-associated protein (mis)folding, aggregation, and the protein homeostasis network?

This is a sample of the questions we address in our research. As tools to obtain more insights, we develop novel protein-based sensors for macromolecular crowding, protein self-association, ionic strength, and others, and apply these inside living cells. In addition, we recreate our findings from living cells inside artificial cells as a much-simplified model where we can control relevant aspects of the living cells. In this manner, we aim to improve our understanding of the molecular (self-)organization.

We engineer proteins, small molecules, and larger cell-like systems for fundamental biological understanding. Our special interest is in sensing and reconstructing intracellular biochemical organization. The biochemical organization includes concepts such as macromolecular crowding and protein self-organization.

Eventually, we aim to apply both our technologies and understanding to applications as medical tools (diagnosis, drug screening).


The group has a strong record of accomplishment in the design of FRET-based protein probes for macromolecular crowding in diverse living and nonliving systems, probes for ionic strength in cells (see left), and probes to determine protein self-organization.

Our research has been made possible by funding from the ERC, NWO, DFG, BMBF, and the Leibniz association 

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