PhD and Postdoctoral Positions at Utrecht Unversity, The Netherlands

Thursday, 20 January 2011 11:44

PhD and Postdoctoral Positions in Proteomics

The Biomolecular Mass Spectrometry and Proteomics Group of prof. Albert Heck (www.hecklab.nl) at Utrecht University is a state of the art laboratory at the core of the Netherlands Proteomics Centre.  For several projects we are seeking graduate level scientists and postdoctoral fellows with advanced degrees in proteomics, bioanalytical chemistry and/or biochemistry/protein chemistry. Keywords that apply to the available projects are enabling technologies, quantitative proteomics, protein modifications, viral proteomics, stem cell proteomics, chemical proteomics and signaling pathways.

Located in the heart of the Netherlands, Utrecht University is one of Europe’s leading research universities, recognized internationally for its high-quality, innovative approach to both research and teaching. The Biomolecular Mass Spectrometry and Proteomics Group forms the core of the Netherlands Proteomics Centre (NPC), a strategic collaboration of proteomics research groups throughout the Netherlands and is coordinator of the European PRIME-XS project, the consortium of leading proteomics facilities and research groups in Europe.

The working language in the lab (and the university) is English. We are looking for individuals who are self-motivated, and enjoy independent work in an interdisciplinary team. To be considered, please send a CV in .pdf  or word form that includes a publication list, a (brief) statement of research interests not exceeding three pages, and three academic references.

For further information please email This e-mail address is being protected from spambots. You need JavaScript enabled to view it

Recent Illustrative work (see also www.hecklab.nl)

  • Comparative assessment of site assignments in CID and electron transfer dissociation spectra of phosphopeptides discloses limited relocation of phosphate groups. Mischerikow N, Altelaar AF, Navarro JD, Mohammed S, Heck AJ. Mol Cell Proteomics. 2010 Oct;9(10):2140-8.
  • Profiling of N-acetylated protein termini provides in-depth insights into the N-terminal nature of the proteome. Helbig AO, Gauci S, Raijmakers R, van Breukelen B, Slijper M, Mohammed S, Heck AJ. Mol Cell Proteomics. 2010 May;9(5):928-39.
  • The leukemia-associated Mllt10/Af10-Dot1l are Tcf4/β-catenin coactivators essential for intestinal homeostasis. Mahmoudi T, Boj SF, Hatzis P, Li VS, Taouatas N, Vries RG, Teunissen H, Begthel H, Korving J, Mohammed S, Heck AJ, Clevers H. PLoS Biol. 2010 Nov 16;8(11):e1000539
  • Phosphorylation dynamics during early differentiation of human embryonic stem cells. Van Hoof D, Muñoz J, Braam SR, Pinkse MW, Linding R, Heck AJ, Mummery CL, Krijgsveld J. Cell Stem Cell. 2009 Aug 7;5(2):214-26.
  • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Boersema PJ, Raijmakers R, Lemeer S, Mohammed S, Heck AJ. Nat Protoc. 2009;4(4):484-94.
  • Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S. Anal Chem. 2009 Jun 1;81(11):4493-501
  • Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes.
  • Mousson F, Kolkman A, Pijnappel WW, Timmers HT, Heck AJ. Mol Cell Proteomics. 2008 May;7(5):845-52