Prof. dr. M. (Marc) Baldus

Nicolaas Bloembergengebouw
Padualaan 12
Kamer 1.14
3584 CH Utrecht

Prof. dr. M. (Marc) Baldus

Professor
NMR Spectroscopy
+31 30 253 3801
m.baldus@uu.nl

Our group develops and applies magnetic resonance (NMR)-based approaches to unravel structure-function relationships in complex molecular systems with the goal to understand principal chemical and biological processes such as signal transduction, molecular transport or (bio)catalysis. We use a combination of solid-state NMR and other spectroscopic and biophysical/cell biology approaches for studies in the following areas:

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 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 how proteins fold and interact with other biomolecules to form complexes. condensates and aggregates. These processes are closely related to biological recognition and diseases such as Parkinson or Alzheimer’s disease and cancer.

Studying molecular interactions in-situ

Ultimately, our goal is to conduct NMR studies in a natural setting. We have pioneered the use of solid-state NMR to examine proteins and other biomolecules inside bacterial and human cells. These studies are directed towards understanding how biomolecular systems are structurally assembled and 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.

 

Our research is funded by National and international Research grants and has been awarded by international prizes, for example by the Association of the European Biophysical Societies or by the International Council on Magnetic Resonance in Biological Systems (ICMRBS).

 

 


Cover of our review article in Angewandte Chem. Int. Ed.
Links
Chair
Structural Biology / NMR Spectroscopy