• Nijenborgh4, Gebouw 5115, ruimte 0308

    9747 AG Groningen

    Netherlands

Persoonlijk profiel

Biosketch

Prof. Dr. Van der Wel did his PhD at the University of Arkansas (USA), in the group of Prof R.E. Koeppe II. After a postdoc in the group of Prof Robert G. Griffin at MIT he started his independent solid-state NMR group at the University of Pittsburgh School of Medicine, reaching the rank of associate professor with tenure. In 2018 he joined the University of Groningen as Associate professor and chair of the Solid-state NMR group. His research focus is the development and application of solid-state NMR spectroscopy as a tool to probe molecular structure and dynamics in (semi)solids and materials. A key interest is the elucidation of disease mechanisms behind (amyloid) protein aggregation diseases and in particular Huntington’s disease. Cutting-edge solid-state NMR measurements have enabled unique insights into the atomic structure of implicated nanometer-sized protein assemblies. Combining NMR and other techniques, the SSNMR group also studies molecular processes implicated in programmed cell death. In collaborative work, they also use SSNMR to analyze a range of (nano)materials. Since coming to Groningen, Prof. Dr. Van der Wel has received funding support from multiple national and international foundations. He is on the board of the Dutch NMRDG network, the European AMPERE committee, as well as advisory board/committees of the Dutch NWO and KNCV. He performs editorial services for the journals Current Research in Structural Biology and PLOS ONE.

Top 3 papers

Lin, H.-K. et al. (2017) ‘Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon 1 rather than its polyglutamine core.’, Nat Commun, 8, p. 15462. Available at: https://doi.org/10.1038/ncomms15462.

This paper reports our discovery of how the Huntington’s disease protein can form different types of toxic protein fibrils, and explains how they differ in structure and dynamics. Our ssNMR analysis reveals an expectedly important role for dynamic surface features.

Li, M. et al. (2019) ‘Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics.’, Structure, 27(5), pp. 806-815.e4. Available at: https://doi.org/10.1016/j.str.2019.02.007.

In this paper we employed our solid-state NMR analysis to show how a nano-sized complex of lipids and proteins is assembled to trigger lipid oxidation in mitochondria. This represents a signal for programmed cell death, with importance for cancer, neurodegeneration and other diseases.

Boatz, J.C. et al. (2020) ‘Protofilament Structure and Supramolecular Polymorphism of Aggregated Mutant Huntingtin Exon 1’, Journal of Molecular Biology, 432(16), pp. 4722–4744. Available at: https://doi.org/10.1016/j.jmb.2020.06.021.

This paper represents a key breakthrough in our understanding the molecular structure of toxic protein deposits from Huntington’s disease. Among several key findings, it presents the most advanced structural model of the nano-sized protein fibrils, enabled by ssNMR analysis.

 

 

 

 

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