Emil Thomasen

Emil Thomasen serves as a Guest Researcher in the Department of Biology within the Biomolecular Sciences unit at the University of Copenhagen's Faculty of Science. His research integrates computational methods with experimental structural biology approaches to investigate complex biomolecular systems.

• Position: Guest Researcher
• Institution: University of Copenhagen
• Department: Department of Biology
• Research Unit: Biomolecular Sciences
• Contact: fe.thomasen@bio.ku.dk | +4535323586

Thomasen's research focuses on developing and applying computational methodologies to understand protein structure, dynamics, and interactions. His work bridges quantum mechanics, molecular dynamics simulations, and experimental techniques including small-angle X-ray scattering (SAXS) and cryo-electron microscopy. He has made significant contributions to coarse-grained modeling, particularly with the Martini force field, and has pioneered approaches combining machine learning with quantum mechanical calculations for large molecular assemblies.

His publication record demonstrates a clear trajectory in computational structural biology, with recent work emphasizing the integration of multiple experimental and computational techniques to characterize complex protein systems. The research shows increasing sophistication in handling large-scale biomolecular assemblies and applying advanced statistical methods like Bayesian inference for model refinement.

Thomasen has established strong collaborative networks, frequently working with Professor K. Lindorff-Larsen and other researchers across computational chemistry and structural biology disciplines. His work has appeared in high-impact journals including Nature Communications, eLife, and Journal of Chemical Theory and Computation.

As a recently completed Ph.D. graduate (2024), Thomasen continues to advance his research program as a Guest Researcher, building on his doctoral work focused on integrating coarse-grained molecular dynamics with SAXS data for characterizing multidomain protein assemblies.