By Jelle Vekeman​

Molecules in liquids are in constant motion, yet out of this apparent chaos emerge the organized structure that underpin chemistry, material science and many natural processes. In this lecture, I will give an overview of how my research uses large‑scale molecular simulations to unravel this hidden organization. I will discuss how molecules in solution find each other, self‑assemble, and initiate the formation of materials such as zeolites and hydrogels. I will also highlight our work on polymer behavior in different solvents, which provides molecular insight relevant to developing more effective strategies for plastic recycling. 

Because these processes unfold across long timescales and involve intricate chemical transformations, I will show how machine‑learning models can accelerate simulations while preserving essential chemical detail. These approaches open the door to studying reactive systems that would otherwise be computationally inaccessible. At the same time, I will address the growing need to reduce the environmental footprint of computational research, and outline how balancing accuracy, computational cost, and energy use can make molecular simulations more sustainable. 

Together, these themes illustrate how fundamental molecular insight, advanced computational methods, and sustainability considerations can reinforce one another. My aim is to show how this combination not only deepens our understanding of molecular behavior, but also supports experimental research and contributes to the design of new, environmentally responsible materials and processes.

By Frederik Lermyte

Proteins are the primary effectors in most biochemical processes, and as such play a major role in everything from industrial applications to human health and disease. It is no surprise then that sophisticated analytical tools have been developed to understand the structure and other properties of proteins. One such method, which has gained prominence in recent years, is mass spectrometry of intact proteins and noncovalent protein complexes. Compared to traditional mass spectrometry of small molecules and peptides, there are of course challenges associated with the gas-phase analysis of these large, fragile structures; however, this method also provides unique opportunities to shed light on the native context of proteins, on the effect of mutations and modifications, and on their three-dimensional structure. In this lecture, I will show some of the contributions my laboratory has made to the further development of these methods and their application in biochemical and biomedical research.