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Frans Mulder


Frans Mulder

Associate Professor Department of Chemistry

Keywords

  • NMR Spectroscopy
  • Biophysics
  • Protein Dynamics
  • Protein Electrostatics
  • Structural Biology

Laboratory for Biomolecular NMR Spectroscopy

Associate Professor Frans A.A. Mulder
PhD in Chemistry

Website

Looking at Nature's Molecules with NMR Spectroscopy

In our group we study protein molecules using nuclear magnetic resonance (NMR) spectroscopy. Proteins are the fantastic products of Nature. Encoded by DNA in our genes, proteins are responsible for the way we look, the way we walk, the way we think. Errors in our proteins spell disease, but proteins are also the key to sustainable energy and novel medicines. Obtaining insight into living organisms at the nanoscale is important to understand the wonders of life at a fundamental level.

NMR spectroscopy is a technique that detects the atomic nuclei inside molecules. NMR can reach deep down and allows us to study molecules on the sub-nanometer (< 0.000001 mm) scale. NMR is a routine technique in chemistry, and is an increasingly important tool in health research, nanoscience and drug design.

At iNANO we use NMR spectroscopy to determine the structures of proteins in their physiological, watery milieu, since 3D structures provide important insights into protein function. We also go one step further, and map out their flexibility, dynamics and electrostatic behavior. The integrative understanding of these fundamental biomolecular properties is essential to achieve a comprehensive understanding of biological processes at the nanoscale.

Our projects focus on the innovation and development of novel techniques and approaches, and we are involved in numerous collaborations with international academic and industrial partners about the application of NMR, ranging from the improvement of barley seed quality to ageing and the molecular basis of Alzheimer’s disease.

Recent publications