Prof. dr. M. (Marc) Baldus

Nicolaas Bloembergengebouw
Padualaan 12
Kamer 1.14
3584 CH Utrecht

Prof. dr. M. (Marc) Baldus

NMR Spectroscopy
030 253 3801

Nuclear Magnetic Resonance (NMR) can provide atomic-level insight into the structure and dynamics of heterogeneous systems. Our group develops NMR-based approaches targeting such molecular arrangements by combining recent advancements in solid-state NMR to enhance spectroscopic sensitivity and resolution with dedicated biochemical and biophysical and cell-biology techniques. Our methods development ranges from NMR pulse schemes and hyperpolarization methods to dedicated labelling and software analysis tools. For further information on our research, please follow the reference links below:

Membrane Proteins seen in functional bilayers and cells

Membrane proteins are critically involved in cell function and cell communication to the exterior and they execute their function in a complex membrane environment. We have been studying ligand binding, structure and dynamics in receptors, ion channels and protein insertion machines. For our studies we use functional bilayer preparations and, more recently, examine membrane proteins in natural bacterial and eukaryotic membranes, membrane envelopes and entire cells.

Understanding protein assembly, condensation and aggregation

A comprehensive atomic-level description of protein folding and assembly which is of paramount biological interest and, at the same time, of great relevance for the design of biomaterials.  We use solid-state NMR and other biophysical methods to study proteins and how they fold and interact with other biomolecules to form complexes. condensates and aggregates. These processes are closely related to biological organization and diseases such as Parkinson’s disease and cancer.

Studying molecular interactions in-situ

Ultimately, our goal is to conduct our studies in natural setting. We have pioneered the use of solid-state NMR to examine proteins and other molecules inside bacterial and human cells. These studies are directed towards understanding how protein structure and assembly are dynamically changing during cellular function and disease. In recent years we also adapted such methods to obtain high-resolution insight into the structural organization of biomaterials and for uncovering the molecular landscape of catalytic reactions in material and life science.