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Biomolecular Mass Spectrometry and Proteomics Group Utrecht University

Contact Details

Utrecht University

Padulaan 8 3584 CH Utrecht

Prof. dr. A.J.R. Heck

0031 (0)30 2535871

Hotel Description

The Biomolecular Mass Spectrometry and Proteomics group of Albert Heck at the Faculty of Science of Utrecht University, consists at present of around 50 people, and is embedded in both the Bijvoet Center for Biomolecular Research of the Department of Chemistry and in the Utrecht Institute for Pharmaceutical Sciences of the Department of Pharmacy. The core research theme of the Heck-group is in the development of mass spectrometric methods applicable to the structural characterization of biomolecular systems, in relation to their biological function. The group houses an excellent array of state-of-the-art mass spectrometers (LTQ-Orbitraps, Q-Exactives, Q-ToF’s, ESI-ToF), combined with extensive protein and peptide separation methods (HPLC, nano-HPLC, chip-based LC, ion-exchange fractionation, size exclusion chromatography, SDS-PAGE) and plays an important role in the Netherlands Proteomics Centre. Within the field of mass spectrometry based proteomics the group focuses on the development of innovative proteomics techniques to improve protein expression quantification, the analysis of membrane proteins, protein post-translational modifications and protein networks. In addition, the group has a world-renown expertise in the analysis of protein-ligand, protein-protein and protein-DNA analysis by mass spectrometry. Therefore, dedicated mass spectrometers and LC methods have been and are developed allowing the analysis of the structure and function of protein machineries with mass spectrometry based structural biology.

  • Biomedical & health
  • Mass-spectrometry based proteomics
  • Mass-spectrometry based structural biology
  • Protein expression quantification
  • Protein post-translational modifications
  • Protein networks;Characterization of protein complexes
  • Next generation proteomics;Bioinformatics for proteomics

Expertise and Track Record

The mass spectrometry and proteomics technology at the research group of Albert Heck is unique in the Netherlands and among the top 3 of proteomics research labs in Europe. The group plays a leading role in the international proteomics field, as evidenced by its coordinating role in European protein mass spectrometry projects and consortia.

  • Koo BK, Spit M, Jordens I, Low TY, Stange DE, van de Wetering M, van Es JH, Mohammed S, Heck AJ, Maurice MM, Clevers H. Tumour suppressor RNF43 is a stem-cell E3 ligase that induces endocytosis of Wnt receptors. Nature. 2012 Aug 30;488(7413):665-9. doi: 10.1038/nature11308. The contribution to this project consisted of all proteomics sample preparation, data acquisition, data analysis and data interpretation.
  • Rose RJ, van Berkel PH, van den Bremer ET, Labrijn AF, Vink T, Schuurman J, Heck AJ, Parren PW. Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG. MAbs. 2013 Feb 13;5(2). The contribution to this project consisted of all protein mass spectrometry sample preparation, data analysis and data interpretation.
  • Côté RG, Griss J, Dianes JA, Wang R, Wright JC, van den Toorn HW, van Breukelen B, Heck AJ, Hulstaert N, Martens L, Reisinger F, Csordas A, Ovelleiro D, Perez-Rivevol Y, Barsnes H, Hermjakob H, Vizcaíno JA. The PRoteomics IDEntification (PRIDE) Converter 2 framework: an improved suite of tools to facilitate data submission to the PRIDE database and the ProteomeXchange consortium. Mol Cell Proteomics. 2012 Dec;11(12):1682-9. doi: 10.1074/mcp.O112.021543.

Albert Heck is since 2003 scientific director of the Netherlands Proteomics Centre (www.netherlandsproteomicscentre.nl) and coordinator of the European proteomics infrastructure PRIME-XS (www.primexs.eu) and the NWO Roadmap project Proteins@Work (www.proteinsatwork.nl) and is involved in the ESFRI project Instruct (www.structuralbiology.eu). The group is also involved in the Netherlands Bioinformatics Centre NBIC and the DTL-DISC and ELIXIR-NL bioinformatics projects.

Hotel Characteristics

  • mass spectrometers, including 6 Orbitraps (of which 4 Exactive and Q-Exactive Orbitraps) and 7 Q-ToF mass spectrometers
  • pprotein and peptide separation methods (2D-gel, DiGE, HPLC, nano-HPLC, chip-based ESI, chip-based LC, SPR, LC-MALDI, scanners)